|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-97 |
3.95e-49 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 169.36 E-value: 3.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 2 KAYLKSPDGFFVLK-KSTTIGKHEdSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHIQNVAVKLIPGD 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGREG-CDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 1958778166 81 ILRFGSSGPTYELVIEN 97
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-1020 |
3.65e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 97.43 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 229 INRLSD--FEMESKYKDaviMNLQAEIA----DLSQRLSEMAAVVAAARqsnrcdprFQDLDEGDDHRQKEIESMKSQIN 302
Cdd:TIGR02168 188 LDRLEDilNELERQLKS---LERQAEKAerykELKAELRELELALLVLR--------LEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 303 ALQKgysqvlsqTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEAL 382
Cdd:TIGR02168 257 ELTA--------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 383 TSRCSKLKEDLRKEEAQ----KERREAQEKELKLCRSQMQDMEKEVKKLREELKknyTGQNVISKTLREKNKLENfRSQV 458
Cdd:TIGR02168 329 ESKLDELAEELAELEEKleelKEELESLEAELEELEAELEELESRLEELEEQLE---TLRSKVAQLELQIASLNN-EIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 459 IKATFGKTKPFRDKPVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNVEKLRVLLDKCQACMRDSCNSM 538
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 539 D-LKKEVELLQHLQLSppVLGLQKAVLNILRvSLSWLEETEQLLGDLnIElsdSDKGFSLCL-IYLLEHYKKIMIQSEel 616
Cdd:TIGR02168 485 AqLQARLDSLERLQEN--LEGFSEGVKALLK-NQSGLSGILGVLSEL-IS---VDEGYEAAIeAALGGRLQAVVVENL-- 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 617 raqvNASLETQQSLQEENLAEKEKLTEKLEQEEKLKAR---IQQLTEEKAALEESVAEEKNKLQGDLEMTQARVH---EL 690
Cdd:TIGR02168 556 ----NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNdreILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvdDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 691 ENDLACQKE-------------------------VLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEkl 745
Cdd:TIGR02168 632 DNALELAKKlrpgyrivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE-- 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 746 kMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITK 825
Cdd:TIGR02168 710 -LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 826 AKMIMAEDRLKLQQQSMKALQDERESQKHGF---EEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSD 902
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 903 SAQKEEVPQEftivpSLDSSAKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELSEKQKTELERQV 982
Cdd:TIGR02168 869 EELESELEAL-----LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
810 820 830
....*....|....*....|....*....|....*...
gi 1958778166 983 ALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREAL 1020
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-84 |
2.17e-16 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 74.53 E-value: 2.17e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778166 18 TTIGKHEDSDLVLQSSDIDNHHALIEFNEaEGTFVLQDFNTRNGTFVNECHIQNVAVKLIPGDILRF 84
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-87 |
6.47e-16 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 74.23 E-value: 6.47e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778166 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNeaEGTFVLQDFNTRNGTFVNECHIQNvAVKLIPGDILRFGSS 87
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVD--GGGVYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDT 87
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
604-883 |
1.86e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 604 EHYKKIMIQSEELRAQVNA----SLETQQSLQEENLAEKEKLTEKLEQE-EKLKARIQQLTEEKAALEESVAEeknkLQG 678
Cdd:COG1196 213 ERYRELKEELKELEAELLLlklrELEAELEELEAELEELEAELEELEAElAELEAELEELRLELEELELELEE----AQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 679 DLEMTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRI 758
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 759 QDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEklslkLKETLAELEITKAKMIMAEDRLKLQ 838
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958778166 839 QQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQ 883
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
612-1104 |
2.09e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 612 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEE----------SVAEEKNKLQGDLE 681
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrreleerleELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 682 MTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTyEKLKMRDTLEKEKRRIQDL 761
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 762 ENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMImAEDRLKLQQQS 841
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAA 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 842 MKALQDERESQKHGFEEEITEYKEQIKQHS----------------------------QTIVNLEERLSQVTQYYRKIEG 893
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeaaleaalaaalqNIVVEDDEVAAAAIEYLKAAKA 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 894 EIATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIACD--------HLIDDLL----MAQKEILSQQEIIMKLRTDLGEAHT 961
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDlreadaryYVLGDTLlgrtLVAARLEAALRRAVTLAGRLREVTL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 962 RMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLS 1041
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778166 1042 QKCDISLQIEPAHPDsfssFQEEQFFSDLGAkckgsrhEEVIQRQKKALSELRTRIKELEKAN 1104
Cdd:COG1196 732 AEREELLEELLEEEE----LLEEEALEELPE-------PPDLEELERELERLEREIEALGPVN 783
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
11-93 |
1.41e-14 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 70.76 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNeaEGTFVLQDFNTRNGTFVNECHIQNvAVKLIPGDILRFGSSGPT 90
Cdd:COG1716 16 FPLDGGPLTIGRAPDNDIVLDDPTVSRRHARIRRD--GGGWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 1958778166 91 YEL 93
Cdd:COG1716 93 FRL 95
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
4-93 |
6.58e-14 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 68.89 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 4 YLKSPDG-FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHI-QNVAVKLIPGDI 81
Cdd:cd22704 3 CLVSSDGtRHRLPRSMLFVGREDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDS 82
|
90
....*....|..
gi 1958778166 82 LRFGSSGPTYEL 93
Cdd:cd22704 83 IRFGYDTNVYRF 94
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
18-85 |
1.33e-11 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 62.25 E-value: 1.33e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 18 TTIGKHEDSDLVLQSSDIDNHHALIEFneAEGTFVLQDFNTRNGTFVNECHI--QNVAVKLIPGDILRFG 85
Cdd:cd22665 23 NVIGRDPSCSVVLPDKSVSKQHACIEV--DGGTHLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFG 90
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
225-900 |
1.52e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 225 LGREINRLSDFEMESKYKD-----AVIMNLQAEIADLSQRLSEMAAVVAAAR-QSNRCDPRFQDLDEGDDHRQKEIESMK 298
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKigeleAEIASLERSIAEKERELEDAEERLAKLEaEIDKLLAEIEELEREIEEERKRRDKLT 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 299 SQINALQKGY-------------SQVLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEV 365
Cdd:TIGR02169 357 EEYAELKEELedlraeleevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 366 NQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQ----EKELKLCRSQMQDMEKEVKKLREELKKNYTGQNVI 441
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEydrvEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 442 SK-------TLRE----------------KNKLENF----------------RSQVIKATFGKTKPFRDKPVTDQQL--- 479
Cdd:TIGR02169 517 KAsiqgvhgTVAQlgsvgeryataievaaGNRLNNVvveddavakeaiellkRRKAGRATFLPLNKMRDERRDLSILsed 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 480 --IERIVQVTEDNLSFQQRKWTLQREThlhskqeEVVHNVEKLRVLLDKCQACMRDScnsmdlkkevELLQHlqlSPPVL 557
Cdd:TIGR02169 597 gvIGFAVDLVEFDPKYEPAFKYVFGDT-------LVVEDIEAARRLMGKYRMVTLEG----------ELFEK---SGAMT 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 558 GLQKAVLNILRVSLSWLEETEQL---LGDLNIELSDsdkgfslcLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEEN 634
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLrerLEGLKRELSS--------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 635 LAEKEKLTEKLEQeekLKARIQQLTEEKAALEesvaEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRKMRE 714
Cdd:TIGR02169 729 EQEEEKLKERLEE---LEEDLSSLEQEIENVK----SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 715 VLEAERRKaqdLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIE-LKGQKEDiLNNKLKdalllv 793
Cdd:TIGR02169 802 KLEEEVSR---IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnLNGKKEE-LEEELE------ 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 794 EDAQQMRTAESTRAEklslkLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQhSQT 873
Cdd:TIGR02169 872 ELEAALRDLESRLGD-----LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEE 945
|
730 740
....*....|....*....|....*..
gi 1958778166 874 IVNLEERLSQVTQYYRKIEGEIATLKD 900
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
280-1022 |
2.60e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.61 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 280 FQDLDEGDDHRQKEIESMKSQINALQKGYSQVLSQTLAERNTEIESLKNEGENlkrdqaitsgMVTSLQKDVSARNEQVQ 359
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEV----------EITGLTEKASSARSQAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 360 QLQEEVN----QLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERR-EAQEKELKLCRSQMQDMEKEVKKLREElKKN 434
Cdd:pfam15921 296 SIQSQLEiiqeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTERDQFSQE-SGN 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 435 YTGQnvISKTLREKNKlenfRSQVIKATFGKTKPFRDKPVTDQQLIERIVQVTEDnlsfqqRKWTLQRETHLhskqeevv 514
Cdd:pfam15921 375 LDDQ--LQKLLADLHK----REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD------RNMEVQRLEAL-------- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 515 hnvekLRVLLDKCQACMRDSCNSMDLKKE-VELLQHL--QLSPPVLGLQKAVLNILRVSLSwLEETEQLLGDLNIELSDS 591
Cdd:pfam15921 435 -----LKAMKSECQGQMERQMAAIQGKNEsLEKVSSLtaQLESTKEMLRKVVEELTAKKMT-LESSERTVSDLTASLQEK 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 592 DKGFSLCLIYLLEHYKKIMIQSEELRAQVNASlETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEekaaleesVAE 671
Cdd:pfam15921 509 ERAIEATNAEITKLRSRVDLKLQELQHLKNEG-DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ--------LVG 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 672 EKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRKMREvLEAerrKAQDLEnqltqqkeisesntYEKLKMRDTL 751
Cdd:pfam15921 580 QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE-LEA---RVSDLE--------------LEKVKLVNAG 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 752 EKEKRRIQDLEnrltKQREEI--ELKGQKEDiLNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMI 829
Cdd:pfam15921 642 SERLRAVKDIK----QERDQLlnEVKTSRNE-LNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 830 MAEDR--------LKLQQQ--SMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLK 899
Cdd:pfam15921 717 SMEGSdghamkvaMGMQKQitAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLR 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 900 DSDSAQKEEVPQeftIVPSLDSSAKEIA-CDHLIddllmaQKEilSQQEIIMKLRTDL------GEAHTRMSDLRGELSe 972
Cdd:pfam15921 797 SQERRLKEKVAN---MEVALDKASLQFAeCQDII------QRQ--EQESVRLKLQHTLdvkelqGPGYTSNSSMKPRLL- 864
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1958778166 973 kQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRA 1022
Cdd:pfam15921 865 -QPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRS 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-898 |
4.01e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 250 QAEIA----DLSQRLSEMAAVVAAARqsnrcdprfqdldegDDHRQKEIESMKSQINALQKGySQVLSQTLAERNTEIES 325
Cdd:COG1196 208 QAEKAeryrELKEELKELEAELLLLK---------------LRELEAELEELEAELEELEAE-LEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 326 LKNEGENLKRDqaitsgmVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREA 405
Cdd:COG1196 272 LRLELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 406 QEKELKLCRSQMQDMEKEVKKLREELKKNYtgQNVISKTLREKNKLENFRSQVIKAtfgktkpfrdkpvtdQQLIERIVQ 485
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAEL--AEAEEELEELAEELLEALRAAAEL---------------AAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 486 VTEDNlsfqqrkwtLQRETHLHSKQEEVVHNVEKLRVLLDKCQAcmrdscnsmDLKKEVELLQHLQLSppVLGLQKAVLN 565
Cdd:COG1196 408 AEEAL---------LERLERLEEELEELEEALAELEEEEEEEEE---------ALEEAAEEEAELEEE--EEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 566 ILRVSLSWLEETEQLLGDLNIELSDSDKgfslcliyLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKL 645
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLL--------LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 646 EQEEKLKARIQQLTEEKAALEESVAEEKNKLQGdlemtqaRVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQD 725
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 726 LENQLTQQKEISESNTYEKLKMRdtlekeKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAEST 805
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAA------LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 806 RAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVT 885
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
650
....*....|...
gi 1958778166 886 QYYRKIEGEIATL 898
Cdd:COG1196 767 RELERLEREIEAL 779
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
19-87 |
5.96e-11 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 60.01 E-value: 5.96e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778166 19 TIGKHEDSDLVLQSSDIDNHHALIEFNEaeGTFVLQDFNTRNGTFVNECHIqNVAVKLIPGDILRFGSS 87
Cdd:cd22693 21 TIGRADDNDLVLSDDFVSSRHARIYLQG--SSWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGAT 86
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
614-912 |
1.83e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 614 EELRAQVNASLETQQSLQEEnlaeKEKLTEKLEQEEKLKARIQQLTEEKAA-LEESVAEEKNKLQGDLEMTQARVHELEN 692
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEE----LEKLTEEISELEKRLEEIEQLLEELNKkIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 693 DLACQKEVLESSVTQEkRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEI 772
Cdd:TIGR02169 309 SIAEKERELEDAEERL-AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 773 ELKGQKEDILNNKLkdalllvEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQ 852
Cdd:TIGR02169 388 KDYREKLEKLKREI-------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 853 KhgfeEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEgeiATLKDSDSAQKEEVPQE 912
Cdd:TIGR02169 461 A----ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE---AQARASEERVRGGRAVE 513
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
274-911 |
4.35e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 274 NRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVS- 352
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEK-INNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 353 ------ARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQ----KERREAQEKELKLCRSQMQDMEK 422
Cdd:TIGR04523 108 inseikNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndlKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 423 EVKKLREELKKNYTGQNVIsKTLREKNKLENFRSQVIKATFGKTKPFRDKPVTDQQLIERIVQVTEDNLsfQQRKWTLQR 502
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNL-KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL--NQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 503 E-THLHSKQEEVVHNVEKLRVLLDKCQacmrdscnsmDLKKEVELLQhlqlsppvlglQKAVLNILRVSLSWLEETEQLL 581
Cdd:TIGR04523 265 IkKQLSEKQKELEQNNKKIKELEKQLN----------QLKSEISDLN-----------NQKEQDWNKELKSELKNQEKKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 582 GDLNIELSDSDKGFSlcliyllehykkimiqseELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEE 661
Cdd:TIGR04523 324 EEIQNQISQNNKIIS------------------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 662 KAALEESVAEEKNKLQGDLEMTQARVHELENdLACQKEVLEssvtQEKRKMREVLEAERRKAQDLENQLTQQKEISESNT 741
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKELLE----KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 742 YEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAEL 821
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 822 EITKAKMIMAEDR-------------------LKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLS 882
Cdd:TIGR04523 541 SDLEDELNKDDFElkkenlekeideknkeieeLKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
650 660
....*....|....*....|....*....
gi 1958778166 883 QVTQYYRKIEGEIATLKDSDSAQKEEVPQ 911
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
11-85 |
8.83e-10 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 56.84 E-value: 8.83e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778166 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNEaEGTFVLQDFNTRNGTFVNECHIQNvAVKLIPGDILRFG 85
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDE-NGKAYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIG 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
605-1370 |
1.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 605 HYKKImiqseELRAQVNASLETQQSLQEENLAEKEKLTE-KLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDL-EM 682
Cdd:PTZ00121 1056 HEGKA-----EAKAHVGQDEGLKPSYKDFDFDAKEDNRAdEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDArKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 683 TQARVHELENDLACQKEVLESSVTQEKRKMREVLEAE-RRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDL 761
Cdd:PTZ00121 1131 EEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEE 1210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 762 ENRLTKQREEIELKGQKEdilnnkLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQ-- 839
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEA------VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElk 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 840 --QSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEiatlKDSDSAQKEEvpqEFTIVP 917
Cdd:PTZ00121 1285 kaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAE---AEAAAD 1357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 918 SLDSSAKEIACDHLIDDLLMAQKEILSQQeiimklrtdlGEAHTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKA 997
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKK----------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 998 KVVQTTGLVEKKDRELKVLREALRASQEKprpylsteQKPRNLSQKCDISLQIEPAHPDSFSSFQEEQffsdlgAKCKGS 1077
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEA--------KKAEEAKKKAEEAKKADEAKKKAEEAKKADE------AKKKAE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1078 RHEEVIQRQKKAlSELRTRIKELEKANSSNHKDHVNESFLELKTLRMEKNVQKILLDAKPDLTTFSRVEIRPPLNGPFSS 1157
Cdd:PTZ00121 1494 EAKKKADEAKKA-AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1158 GSpfamEKSMKTDAAEALELSEKlytdmiKTLGSLMNIKDMSSHMSLKHLSPKERERVNHLRQKDLDLVFDKITQLKtrl 1237
Cdd:PTZ00121 1573 EE----DKNMALRKAEEAKKAEE------ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK--- 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1238 QRKEELVRgyewELEQLRHSKVSVQMYQTQVAKLEDDIHKEAEEKALLKEALDRTEQQLSQEKRLNRAFKQQKDRVEDQE 1317
Cdd:PTZ00121 1640 KKEAEEKK----KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1318 QRNSScscpFKENEKQRRIFVEMVKRKMQDSSLQA-------GAKKATLKTGQERETKKE 1370
Cdd:PTZ00121 1716 KKAEE----LKKAEEENKIKAEEAKKEAEEDKKKAeeakkdeEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
638-1022 |
1.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 638 KEKLTEKLEQ-EEKLkARIQQLTEEKAA----LEE--SVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKR 710
Cdd:COG1196 174 KEEAERKLEAtEENL-ERLEDILGELERqlepLERqaEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 711 KMREVLEAERRKaqdLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDAL 790
Cdd:COG1196 253 AELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 791 LLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQkhgfEEEITEYKEQIKQH 870
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 871 SQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVpqeftivpsldssakeiacDHLIDDLLMAQKEILSQQEIIM 950
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-------------------EEAAEEEAELEEEEEALLELLA 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958778166 951 KLRTDLGEAHTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRA 1022
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
236-851 |
1.57e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 236 EMESKYKDAVIMNLQAEIADLSQRLSEMAAVVAAARQsnrcdpRFQDLDEG-DDHRQK--EIESMKSQINALQKGYSQV- 311
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARE------TRDEADEVlEEHEERreELETLEAEIEDLRETIAETe 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 312 -----LSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRC 386
Cdd:PRK02224 272 rereeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 387 SKLKEdlRKEEAQKERREAqEKELKLCRSQMQDMEKEVKKLREELKknytgqnviskTLREKnklenfrsqvikatfgkt 466
Cdd:PRK02224 352 DDLEE--RAEELREEAAEL-ESELEEAREAVEDRREEIEELEEEIE-----------ELRER------------------ 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 467 kpFRDKPVTDQQLIERIVQVTEDnlsfqqRKWTLQRETHLHSKQEEVVHNVEKLRVLLD--KCQACMrdscnsmdlkkev 544
Cdd:PRK02224 400 --FGDAPVDLGNAEDFLEELREE------RDELREREAELEATLRTARERVEEAEALLEagKCPECG------------- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 545 ellQHLQLSPPVLGLqkavlnilrvslswlEETEQLLGDLNIELSDsdkgfslcliyllehykkimiqseelraqvnasL 624
Cdd:PRK02224 459 ---QPVEGSPHVETI---------------EEDRERVEELEAELED---------------------------------L 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 625 ETQQSLQEENLAEKEKLTEkleqeekLKARIQQLTEEKAALEESVAEEKNKLQGD---LEMTQARVHELENDLACQKEvl 701
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVE-------AEDRIERLEERREDLEELIAERRETIEEKrerAEELRERAAELEAEAEEKRE-- 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 702 essvtqEKRKMREVLEAERRKAQDLENQLTQQKEISES-NTYEKL-----KMRDTLEKEKRRIQDLENRLTKQREEIELK 775
Cdd:PRK02224 559 ------AAAEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLlaaiaDAEDEIERLREKREALAELNDERRERLAEK 632
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778166 776 GQKEDILNNKLKDAllLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKlqqqSMKALQDERES 851
Cdd:PRK02224 633 RERKRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE----ELEELRERREA 702
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
15-85 |
2.12e-09 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 55.96 E-value: 2.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778166 15 KKSTTIGKHEDSDLVLQSSDIDNHHALIEFnEAEGTFVLqDFNTRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22683 20 RNVTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
349-772 |
8.60e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 349 KDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEkELKLCRSQMQDMEKEVKKLR 428
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 429 EELKKNYTGQNVISKTLREKNKLENFRSQVIKATFGKTKPFRDKPVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHS 508
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 509 KQEEVVHNVEKLRVLLdkcqacmrdscnSMDLKKEVELLQHLQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLNIEL 588
Cdd:COG4717 240 ALEERLKEARLLLLIA------------AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 589 SDSDKGFSLCLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEEnLAEKEKLTEKLEQEEkLKARIQQLTEEKAALEES 668
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELEEELQLEE-LEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 669 VAEEKNKLQGDLEMTQARVHELENDLACQ-KEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQ-QKEISE-SNTYEKL 745
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELlGELEELLEALDEEELEEELEELEEELEELEEELEElREELAElEAELEQL 465
|
410 420
....*....|....*....|....*..
gi 1958778166 746 KMRDTLEKEKRRIQDLENRLTKQREEI 772
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEW 492
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
556-1125 |
9.73e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 556 VLGLQKAVLNILRVSLSWLEETE--QLLGDLNIELSDSDKgfslcliyLLEHYkkimiqsEELRAQVNASLETQQSLQEE 633
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDE--------EIERY-------EEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 634 NLAEKEKLTEkLEQE-EKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRK- 711
Cdd:PRK02224 246 HEERREELET-LEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDe 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 712 -MREVLEAERRKAQDLENQltqqkeiSESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDAL 790
Cdd:PRK02224 325 eLRDRLEECRVAAQAHNEE-------AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 791 LLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQsmkaLQDERESQKHGFEEEITEYKEQIKQH 870
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA----LLEAGKCPECGQPVEGSPHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 871 SQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEevpqeftiVPSLDSSAKEIacDHLIDDllmAQKEILSQQEIIM 950
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR--------IERLEERREDL--EELIAE---RRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 951 KLRTDLGEAHTRMSDLRgELSEKQKTELERQVALVRQQNSELSILK------AKVVQTTGLVEKKDRELKVLREALRASQ 1024
Cdd:PRK02224 541 ELRERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAELKerieslERIRTLLAAIADAEDEIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1025 EKprpylsTEQKPRNLSQKCDISLQIEpahpdsfSSFQEEQFfsdLGAKCKGSRHEEVIQRQKKALSELRTRIKELEKAN 1104
Cdd:PRK02224 620 EL------NDERRERLAEKRERKRELE-------AEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
570 580
....*....|....*....|.
gi 1958778166 1105 SSnhkdhVNESFLELKTLRME 1125
Cdd:PRK02224 684 GA-----VENELEELEELRER 699
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
636-1119 |
1.62e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 636 AEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAE---EKNKLQGDLEMTQARVHELE------NDLACQKEVLESSVT 706
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINEissELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 707 QEKRKMREV---LEAERRKAQDLENQLTQQKEISES-NTYEKL-KMRDTLEKEKRRIQDLENRLTKQREEIELKGQKedi 781
Cdd:PRK03918 256 KLEEKIRELeerIEELKKEIEELEEKVKELKELKEKaEEYIKLsEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 782 LNNKlkdalllvedaqqmrtaeSTRAEKLSLKLKETLAELEITKAKMIMAEDrlklqqqsMKALQDERESQKHGFE-EEI 860
Cdd:PRK03918 333 LEEK------------------EERLEELKKKLKELEKRLEELEERHELYEE--------AKAKKEELERLKKRLTgLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 861 TEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDS------------------DSAQKEEVPQEFTIvpSLDSS 922
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcgrelTEEHRKELLEEYTA--ELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 923 AKEIA-CDHLIDDLLMAQKEI---LSQQEIIMKLRTDLGEahtrMSDLRGELSEKQKTELERQVALVRQQNSELSILKAK 998
Cdd:PRK03918 465 EKELKeIEEKERKLRKELRELekvLKKESELIKLKELAEQ----LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 999 VVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLSQKCDISL-----QIEPAHPDSFSSFQEEQFFSDLGAK 1073
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELeerlkELEPFYNEYLELKDAEKELEREEKE 620
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958778166 1074 CKGSRHE-----EVIQRQKKALSELRTRIKELEKANSSNHKDHVNESFLEL 1119
Cdd:PRK03918 621 LKKLEEEldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
215-1028 |
2.18e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 59.21 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 215 QQDKDDIILLLGREINRLSDFEMESKykdavimnlQAEIADLSQRLSEMAAVVAAARQSNRCDPRFQDLDEGDDHRQKEI 294
Cdd:pfam02463 183 ENLAELIIDLEELKLQELKLKEQAKK---------ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 295 ESMKSQINALQKGYSQVLsQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQL-RIQNK 373
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVL-KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAeKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 374 EKEYQLEALTSrcskLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKnytGQNVISKTLREKNKLEN 453
Cdd:pfam02463 333 EKEEIEELEKE----LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS---AAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 454 FRSQVIKAtfgktkpfrdkpvtdQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNVEKLRVLLDKCQACMRD 533
Cdd:pfam02463 406 EAQLLLEL---------------ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 534 SCNSMDLKKEVELLQHLQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKIMIQS 613
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 614 EELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELEND 693
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 694 LACQKEVLESSVTQEKRKMREV-LEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEI 772
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 773 ELKGQKEDILNNKLKDALLLVEDAQQmrtaestRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDEResq 852
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINE-------ELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER--- 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 853 khgfEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEI-ATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIACDHL 931
Cdd:pfam02463 781 ----EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEeQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 932 IDDLLMAQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELSEKQKTELERQVALvRQQNSELSILKAKVVQTTGLVEKKDR 1011
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL-NLLEEKENEIEERIKEEAEILLKYEE 935
|
810
....*....|....*..
gi 1958778166 1012 ELKVLREALRASQEKPR 1028
Cdd:pfam02463 936 EPEELLLEEADEKEKEE 952
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
291-952 |
2.33e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 291 QKEIESMKSQINALQKGYSQvLSQTLAERNTEIESL-KNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLR 369
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 370 IQNKEKEYQLEALTSRcskLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNytgQNVISKTLREKN 449
Cdd:TIGR02169 329 AEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY---REKLEKLKREIN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 450 KLENFRSQVIKATFGKTKPFRDKPVTDQQLIERIVQVTEDNLSFQQRKWTLQRETH---------------LHSKQEEVV 514
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEqlaadlskyeqelydLKEEYDRVE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 515 HNVEKLRVLLDKCQACMRDSCNSMDLKKEVELLqhlqLSPPVLGLQKAVLNILRVSLSWLEETEQLLGD-LNIELSDSDK 593
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERVRGGRAVEEV----LKASIQGVHGTVAQLGSVGERYATAIEVAAGNrLNNVVVEDDA 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 594 GFSLCLIYLLEHYKKIM-------IQSEELraQVNASLETQQSLQEENLAEKEK--------------LTEKLEQEEKLK 652
Cdd:TIGR02169 559 VAKEAIELLKRRKAGRAtflplnkMRDERR--DLSILSEDGVIGFAVDLVEFDPkyepafkyvfgdtlVVEDIEAARRLM 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 653 ARIQQLTEEKAALEESVA------------EEKNKLQGDLEMTQARVHELENDLA-CQKEV--LESSVTQEKRKM----R 713
Cdd:TIGR02169 637 GKYRMVTLEGELFEKSGAmtggsraprggiLFSRSEPAELQRLRERLEGLKRELSsLQSELrrIENRLDELSQELsdasR 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 714 EVLEAERRKAQDLENQLTQQKEISESNTY------EKLKMRDTLEKEKRRIQDLENRLTKQREEIE-----LKGQKEDIL 782
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDlssleqEIENVKSELKELEARIEELEEDLHKLEEALNdlearLSHSRIPEI 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 783 NNKLKDalLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEdrLKLQQQSMKALQDERESQKHGFEEEITE 862
Cdd:TIGR02169 797 QAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID--LKEQIKSIEKEIENLNGKKEELEEELEE 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 863 YKEQIKQH-------SQTIVNLEERLSQVTQYYRKIEGEIATLKDSDS---AQKEEVPQEFT-IVPSLDSSAKEIACDHL 931
Cdd:TIGR02169 873 LEAALRDLesrlgdlKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkAKLEALEEELSeIEDPKGEDEEIPEEELS 952
|
730 740
....*....|....*....|.
gi 1958778166 932 IDDLlmaQKEILSQQEIIMKL 952
Cdd:TIGR02169 953 LEDV---QAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
707-1034 |
3.44e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 707 QEKRKMRE----VLEAERRKAQDLEN--QLTQQKEISESNTYEKLKMRDTLEKEK----------RRIQDLE-------- 762
Cdd:TIGR02169 153 VERRKIIDeiagVAEFDRKKEKALEEleEVEENIERLDLIIDEKRQQLERLRRERekaeryqallKEKREYEgyellkek 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 763 NRLTKQREEI--ELKGQKEDI--LNNKLKDALLLVEDAQQMRTAESTRAEKLS----LKLKETLAELEITKAKMIMAEDR 834
Cdd:TIGR02169 233 EALERQKEAIerQLASLEEELekLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 835 LKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFT 914
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 915 IVPSLDSSAKEI--ACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELsEKQKTELERQVALVRQQNSEL 992
Cdd:TIGR02169 393 KLEKLKREINELkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLAADLSKYEQEL 471
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958778166 993 SILKAKVVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTE 1034
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
5-94 |
3.57e-08 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 52.33 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 5 LKSPDGFFVLK--KSTTIGKHEDSDLVLQSSDIDNHHALIEFneAEGTFVLQDFNTRNGTFVNECHIQnvAVKLIPGDIL 82
Cdd:cd22694 3 IRIPGGELRFDpgSSVRIGRDPDADVRLDDPRVSRRHALLEF--DGDGWVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRV 78
|
90
....*....|....
gi 1958778166 83 RFG--SSGPTYELV 94
Cdd:cd22694 79 RLGdpTDGPALTVV 92
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
24-93 |
5.84e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438777 [Multi-domain] Cd Length: 106 Bit Score: 52.24 E-value: 5.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778166 24 EDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHIQN---VAVKLipGDILRFGSSGPTYEL 93
Cdd:cd22725 28 EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
24-85 |
6.24e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438776 [Multi-domain] Cd Length: 106 Bit Score: 51.90 E-value: 6.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778166 24 EDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHI-QNVAVKLIPGDILRFG 85
Cdd:cd22724 28 DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
694-910 |
8.05e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 694 LACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESntyEKLKMRDTLEKEKRRIQDLENRLTKQREEIE 773
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---QLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 774 LKGQKEDILNNKLK----------------------DALLLVEDAQQM-RTAESTRAekLSLKLKETLAELEITKAKMIM 830
Cdd:COG4942 87 ELEKEIAELRAELEaqkeelaellralyrlgrqpplALLLSPEDFLDAvRRLQYLKY--LAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 831 AEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVP 910
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
351-871 |
8.33e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 351 VSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKlcrsQMQDMEKEVKKLREE 430
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 431 LKKNYTGQNVISKTLREKNKLENFRSQVIKATFGKTKPFRDKPVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLhsKQ 510
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL--KK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 511 EEVVHNVEKLRVLLDKCQacmrdscnsmdlKKEVELLQHLQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLNIELSD 590
Cdd:PRK03918 380 RLTGLTPEKLEKELEELE------------KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 591 SDKG-----FSLCLIYLLEHYKKIMIQSEELRAQVnASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAAL 665
Cdd:PRK03918 448 EHRKelleeYTAELKRIEKELKEIEEKERKLRKEL-RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 666 EESVAEEKNKLQGDLEMTQARVHELEnDLACQKEVLESSVTQEKRKMREVLEAERRKA----QDLENQLTQQKEIseSNT 741
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPF--YNE 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 742 YEKLK-MRDTLEKEKRRIQDLENRLTKQREEI--------ELKGQKEDILNN-------KLKDALLLVEDAQQMRTAEST 805
Cdd:PRK03918 604 YLELKdAEKELEREEKELKKLEEELDKAFEELaetekrleELRKELEELEKKyseeeyeELREEYLELSRELAGLRAELE 683
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778166 806 RAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDEResqkhgfeEEITEYKEQIKQHS 871
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELR--------EKVKKYKALLKERA 741
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
324-433 |
1.58e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 56.02 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 324 ESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEaqKERR 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI--RKDR 465
|
90 100 110
....*....|....*....|....*....|..
gi 1958778166 404 EAQ--EKELKLCRSQMQDMEKEVKKLREELKK 433
Cdd:COG2433 466 EISrlDREIERLERELEEERERIEELKRKLER 497
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
15-87 |
1.97e-07 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 50.63 E-value: 1.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778166 15 KKSTTIGKHEDSDLVLQSSDIDNHHALIEFN----EAEGTFVLQDFNTRNGTFVNECHIQ-NVAVKLIPGDILRFGSS 87
Cdd:cd22677 21 KSFYVFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFGGS 98
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
18-65 |
2.47e-07 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 48.71 E-value: 2.47e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958778166 18 TTIGKHE-DSDLVLQSSDIDNHHALIEFNEaEGTFVLQDFNTRNGTFVN 65
Cdd:smart00240 1 VTIGRSSeDCDIQLDGPSISRRHAVIVYDG-GGRFYLIDLGSTNGTFVN 48
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
321-1004 |
3.03e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 321 TEIESLKNEGENLKRDqaiTSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRcSKLKEDLRKEEAQK 400
Cdd:TIGR00618 194 GKAELLTLRSQLLTLC---TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 401 ERREAQEKELKLCRSQMQDMEK------EVKKLREELKKNYTGQNVISKTLREKNKLENFRSQVIKATFGKTKPFRDKPV 474
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 475 TDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNVEKLRVLLDKCQACMRDSCNSMDLKKEVELLQ-HLQLS 553
Cdd:TIGR00618 350 LHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQgQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 554 PPVLGLQKAVLNILRVSlswLEETEQLLGDLNIELSDSDKGFSlCLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQ-- 631
Cdd:TIGR00618 430 KKQQELQQRYAELCAAA---ITCTAQCEKLEKIHLQESAQSLK-EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcp 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 632 -EENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESvaEEKNKLQGDLEMTQARVHELENDLACQKE-VLESSVTQEK 709
Cdd:TIGR00618 506 lCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS--EEDVYHQLTSERKQRASLKEQMQEIQQSFsILTQCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 710 RKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDA 789
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 790 LLLVEDAQ----QMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKL-------QQQSMKALQDERESQKHGFEE 858
Cdd:TIGR00618 664 ALSIRVLPkellASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEydrefneIENASSSLGSDLAAREDALNQ 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 859 EITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIACDHLidDLLMA 938
Cdd:TIGR00618 744 SLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE--DILNL 821
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778166 939 QKEILSQQEiiMKLRTDLGEAHTRMSDLRGELSE-----KQKTELERQVALVRQQNSELSILKAKVVQTTG 1004
Cdd:TIGR00618 822 QCETLVQEE--EQFLSRLEEKSATLGEITHQLLKyeecsKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDG 890
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
310-883 |
3.16e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 310 QVLSQTLAERNTEIESLKNEGENLKRDQAitsgmvtslqkDVSARNEQVQQLQEEVNQLRIQNkEKEYQLEALTSRCSKL 389
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQS-----------SIEEQRRLLQTLHSQEIHIRDAH-EVATSIREISCQQHTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 390 KEDLRKEEAQKERREAQEKELKLCRSQMQdmEKEVKKLREELKKNYTGQNVISKTLREKNKLENFRSQVIKATfgktkpf 469
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQ--REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT------- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 470 rdkpVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHsKQEEVVHNVEKLRVLLDKCQACMRDscnsmdlKKEVELLQH 549
Cdd:TIGR00618 449 ----CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH-LQETRKKAVVLARLLELQEEPCPLC-------GSCIHPNPA 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 550 LQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLnIELSDSDKGFSLCLIYLLEHYKKIMIQSEELRAQVNASLETQQS 629
Cdd:TIGR00618 517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQL-TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 630 LQE--ENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEknklqgdLEMTQARVHELENDLACQKEVLES-SVT 706
Cdd:TIGR00618 596 LQDltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE-------LALKLTALHALQLTLTQERVREHAlSIR 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 707 QEKRKMREVLEAERRKAQDLENQLTQQKEISEsntYEKLKMRDTLEKEK---RRIQDLENRLTKQREEIElkgQKEDILN 783
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYWKEMLA---QCQTLLRELETHIEeydREFNEIENASSSLGSDLA---AREDALN 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 784 NKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEY 863
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
570 580
....*....|....*....|
gi 1958778166 864 KEQIKQHSQTIVNLEERLSQ 883
Cdd:TIGR00618 823 CETLVQEEEQFLSRLEEKSA 842
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
624-914 |
4.56e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.13 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 624 LETQQSLQEENLAEKEKLTEKLEQEEKlkariqqlteEKAALEESVAEEKNKLQGDLEMTQARVHELENDLAC------Q 697
Cdd:pfam07888 78 LESRVAELKEELRQSREKHEELEEKYK----------ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTltqrvlE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 698 KEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQ 777
Cdd:pfam07888 148 RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 778 KEDILNNKLKDALLLVEDAQ-QMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQD------ERE 850
Cdd:pfam07888 228 KEAENEALLEELRSLQERLNaSERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGrarwaqERE 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958778166 851 SQKHGFEEEiteyKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFT 914
Cdd:pfam07888 308 TLQQSAEAD----KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQ 367
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
322-1043 |
5.37e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 322 EIESLKNEGENLKRDQA---ITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQnKEKEYQ--LEALTSRCSKLKEDLRKE 396
Cdd:pfam12128 242 EFTKLQQEFNTLESAELrlsHLHFGYKSDETLIASRQEERQETSAELNQLLRT-LDDQWKekRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 397 EAQKERREAQEK--------ELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISK---TLREKNKLENFRsqVIKATFGK 465
Cdd:pfam12128 321 RSELEALEDQHGafldadieTAAADQEQLPSWQSELENLEERLKALTGKHQDVTAkynRRRSKIKEQNNR--DIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 466 TKPFRDKpvtdqqlIERIVQVTEDNLSFQQRKWTLQRE---THLHSKQEEVVHNVEKLRVLLDKCQAC---------MRD 533
Cdd:pfam12128 399 LAKIREA-------RDRQLAVAEDDLQALESELREQLEagkLEFNEEEYRLKSRLGELKLRLNQATATpelllqlenFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 534 SCNSMDLKKEVELLQHLQLSPPVLGLQKA---VLNILRVSLSWLEETEQLLGDLNIELSDSdkgfSLCLIYLL------- 603
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRrdqASEALRQASRRLEERQSALDELELQLFPQ----AGTLLHFLrkeapdw 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 604 -EHYKKIMIQSEELRAQVNASLETQQSLQEENLAekekltekleqeeKLKARIQQL-TEEKAALEESVAEEKNKLQGDLE 681
Cdd:pfam12128 548 eQSIGKVISPELLHRTDLDPEVWDGSVGGELNLY-------------GVKLDLKRIdVPEWAASEEELRERLDKAEEALQ 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 682 MTQARVHELENDLAcqkevlessvtQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDL 761
Cdd:pfam12128 615 SAREKQAAAEEQLV-----------QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANER 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 762 ENRLTKQREEIELKGQkedilnnklkdaLLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQS 841
Cdd:pfam12128 684 LNSLEAQLKQLDKKHQ------------AWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKA 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 842 MKAlQDERESQKHGFEEE-ITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFtivpsld 920
Cdd:pfam12128 752 LET-WYKRDLASLGVDPDvIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI------- 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 921 sSAKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELSEKQKTELERQVAL-VRQQNSELSILKAKV 999
Cdd:pfam12128 824 -SELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGsIGERLAQLEDLKLKR 902
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1958778166 1000 VQTTGLVEKKDRELKVLREALRASqEKPRPYLSTEQKPRNLSQK 1043
Cdd:pfam12128 903 DYLSESVKKYVEHFKNVIADHSGS-GLAETWESLREEDHYQNDK 945
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
5-93 |
6.38e-07 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438743 [Multi-domain] Cd Length: 113 Bit Score: 49.34 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 5 LKSPDGFFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHIQ-NVAVKLIPGDILR 83
Cdd:cd22691 18 LHGKFSKSEEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVR 97
|
90
....*....|
gi 1958778166 84 FGSSGPTYEL 93
Cdd:cd22691 98 LGASTRVYRL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-695 |
8.88e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 318 ERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEE 397
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 398 AQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISKTLREKnkLENFRSQVikatfgktkpfrdkpvtdq 477
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA--LDELRAEL------------------- 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 478 qlierivqvTEDNLSFQQRKWTLQR-ETHLHSKQEEVVHNVEKLRvlldkcqacmrdscnsmDLKKEVELLQHLqlsppv 556
Cdd:TIGR02168 813 ---------TLLNEEAANLRERLESlERRIAATERRLEDLEEQIE-----------------ELSEDIESLAAE------ 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 557 lglqkavlnilrvslswLEETEQLLGDLNIELSDsdkgfslcliyLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLA 636
Cdd:TIGR02168 861 -----------------IEELEELIEELESELEA-----------LLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 637 EKEKLTEKLEQEEKLKARIQ-----------QLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLA 695
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEglevridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
697-832 |
1.08e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 697 QKEVLEssVTQEKRKMREVLEAE----RRKAQDLENQLTQQKEISEsntyeklKMRDTLEKEKRRIQDLENRLTKQREEI 772
Cdd:PRK12704 56 KEALLE--AKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLD-------RKLELLEKREEELEKKEKELEQKQQEL 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 773 ELKGQKEDILNNKLKDAL-----LLVEDAQQM---RTAESTRAEKLSL-KLKETLAELEITK-AKMIMAE 832
Cdd:PRK12704 127 EKKEEELEELIEEQLQELerisgLTAEEAKEIlleKVEEEARHEAAVLiKEIEEEAKEEADKkAKEILAQ 196
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
317-865 |
1.15e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 317 AERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKE------KEYQLEALTSRCSKLK 390
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadeakkKAEEKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 391 EDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKnytGQNVISKTLREKNKLENFRsqviKATFGKTKPFR 470
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK---ADEAKKKAEEAKKKADEAK----KAAEAKKKADE 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 471 DKPVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNVEKLRVLldkcQACMRDSCNSMDLKKEVELLQhl 550
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKK-- 1588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 551 qlsppvlgLQKAvlNILRVSLSWLEETEQLLGDLNIELSDSDKGFSLcliYLLEHYKKIMIQSEELRAQVNASLETQQSL 630
Cdd:PTZ00121 1589 --------AEEA--RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 631 QEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKR 710
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 711 KMREvlEAERRKAQDL------ENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNN 784
Cdd:PTZ00121 1736 KKEA--EEDKKKAEEAkkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEG 1813
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 785 KlKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEitkaKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYK 864
Cdd:PTZ00121 1814 G-KEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE----KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD 1888
|
.
gi 1958778166 865 E 865
Cdd:PTZ00121 1889 E 1889
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
19-87 |
1.20e-06 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 48.13 E-value: 1.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778166 19 TIGKHEDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVN--ECHIQNVAVKLIPGDILRFGSS 87
Cdd:cd22678 26 TIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGSE 96
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
604-1127 |
1.36e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 604 EHYKKIMiqsEELRAQVNaslETQQSLQEEN-LAEKEKLTEKlEQEEKLKARIQQLTEEKAALEEsVAEEKNKLQGDLE- 681
Cdd:pfam15921 74 EHIERVL---EEYSHQVK---DLQRRLNESNeLHEKQKFYLR-QSVIDLQTKLQEMQMERDAMAD-IRRRESQSQEDLRn 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 682 MTQARVHELENDLACQKEVLESSVTQEKrKMREVLEAERRKAQDLENQLTQQKEISESNTYEK---------------LK 746
Cdd:pfam15921 146 QLQNTVHELEAAKCLKEDMLEDSNTQIE-QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHdsmstmhfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 747 MRDTLEKE----KRRIQDLENRLTKQREE----IELKGQK-----EDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLK 813
Cdd:pfam15921 225 ILRELDTEisylKGRIFPVEDQLEALKSEsqnkIELLLQQhqdriEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 814 LKET----------LAELEITKAKMimaEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQ 883
Cdd:pfam15921 305 QEQArnqnsmymrqLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 884 VTQYYRKIEGEIATLKDSDSAQKEEvpqeftivpsldSSAKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL-GEAHTR 962
Cdd:pfam15921 382 LLADLHKREKELSLEKEQNKRLWDR------------DTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 963 MSDLRGelsekQKTELERQVALVRQQNSELSILKAKVVQTTG---LVEKKDRELKVLREALrasQEKPRPYLSTEQKPRN 1039
Cdd:pfam15921 450 MAAIQG-----KNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmTLESSERTVSDLTASL---QEKERAIEATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1040 LSQKCDISLQiEPAHPDSfssfqEEQFFSDLGAKCKGSRHE--------EVIQRQKKALSEL---RTRIKELEKANSSNH 1108
Cdd:pfam15921 522 LRSRVDLKLQ-ELQHLKN-----EGDHLRNVQTECEALKLQmaekdkviEILRQQIENMTQLvgqHGRTAGAMQVEKAQL 595
|
570
....*....|....*....
gi 1958778166 1109 KDHVNESFLELKTLRMEKN 1127
Cdd:pfam15921 596 EKEINDRRLELQEFKILKD 614
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
20-93 |
1.63e-06 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 48.06 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 20 IGKHED-SDLVLQSSDIDNHHALIEF----NEAEGTFVLQ------DFNTRNGTFVNECHIQ-NVAVKLIPGDILRFGSS 87
Cdd:cd22676 25 IGRDRRvADIPLDHPSCSKQHAVIQFreveKRNEGDVIENirpyiiDLGSTNGTFLNGEKIEpRRYYELREKDVLKFGLS 104
|
....*.
gi 1958778166 88 GPTYEL 93
Cdd:cd22676 105 TREYVL 110
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
612-812 |
2.26e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 612 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQeekLKARIQQLTEEKAALEEsvaeEKNKLQGDLEMTQARVHELE 691
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA---LERRIAALARRIRALEQ----ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 692 NDLACQKEVLE----------------------------------SSVTQEKRKMREVLEAERRKAQDLENQLTQQKEIS 737
Cdd:COG4942 97 AELEAQKEELAellralyrlgrqpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778166 738 ESNTYEKLKMRDTLEKEKRR----IQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSL 812
Cdd:COG4942 177 EALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
18-85 |
2.46e-06 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438736 [Multi-domain] Cd Length: 94 Bit Score: 46.99 E-value: 2.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778166 18 TTIGKHEDSDLVLQSSDIDNHHAliEFNEAEGTFVLQDFNTRNGTFVNECHIQnvAVKLIPGDILRFG 85
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHA--EFRRAEGGFVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIG 86
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
620-1051 |
3.38e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 620 VNASLETQQSLQEENLAEKEKLTEKleQEEKLKARIQQLTEEKAALEESVAEEKNKlQGDLEMTQARVHELENDLACQKE 699
Cdd:pfam05483 350 VVTEFEATTCSLEELLRTEQQRLEK--NEDQLKIITMELQKKSSELEEMTKFKNNK-EVELEELKKILAEDEKLLDEKKQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 700 V--LESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQD---------LENRLTKQ 768
Cdd:pfam05483 427 FekIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdkllLENKELTQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 769 REE---IELKGQKEDILNNKlkdalllvedaqqmrtaestRAEKLSLKLKETLAELEIT-KAKMIMAEDRLKLQQQSMKA 844
Cdd:pfam05483 507 EASdmtLELKKHQEDIINCK--------------------KQEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEVKC 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 845 LQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLD---S 921
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElelA 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 922 SAKEiACDHLIDDLlmaQKEILSQQEIIMKLRTDLGEAHTRMSD---LRGELSEKQKTELERQVALVRQQNSELSILKAK 998
Cdd:pfam05483 647 SAKQ-KFEEIIDNY---QKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEE 722
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958778166 999 VVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLSQKCDISLQIE 1051
Cdd:pfam05483 723 RDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
250-850 |
3.72e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 250 QAEIADLSQRLSEMAAVVAAA-RQSNRCDPRFQDLDEGDDHRQKEIESMKSQInalqkGYSQVLSQTLAERNTEIESLKN 328
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETeREREELAEEVRDLRERLEELEEERDDLLAEA-----GLDDADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 329 EGENLKRDQAItsgmvtslqkDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEeaqkerreaqek 408
Cdd:PRK02224 325 ELRDRLEECRV----------AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR------------ 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 409 elklcRSQMQDMEKEVKKLREElkknytgqnvisktlreknklenfrsqvikatfgktkpFRDKPVTDQQLIERIVQVTE 488
Cdd:PRK02224 383 -----REEIEELEEEIEELRER--------------------------------------FGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 489 DnlsfqqRKWTLQRETHLHSKQEEVVHNVEKLRVLLD--KCQACMrdscnsmdlkkevellQHLQLSPPVLGlqkavlni 566
Cdd:PRK02224 420 E------RDELREREAELEATLRTARERVEEAEALLEagKCPECG----------------QPVEGSPHVET-------- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 567 lrvslswLEETEQLLGDLNIELSDsdkgfslcliyllehykkimiqSEELRAQVNASLETQQSLQE-----ENLAEKEKL 641
Cdd:PRK02224 470 -------IEEDRERVEELEAELED----------------------LEEEVEEVEERLERAEDLVEaedriERLEERRED 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 642 TEKL--EQEEKLKA---RIQQLTEEKAALEESvAEEK----NKLQGDLEMTQARVHELENDLACQKEVLESSvtqekRKM 712
Cdd:PRK02224 521 LEELiaERRETIEEkreRAEELRERAAELEAE-AEEKreaaAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 713 REVLEAERRKAQDLENQLTQQKEISESNTYEklkmRDTLEKEKRRIQDLENRLTKQREEiELKGQKEdilnnKLKDALLL 792
Cdd:PRK02224 595 RTLLAAIADAEDEIERLREKREALAELNDER----RERLAEKRERKRELEAEFDEARIE-EAREDKE-----RAEEYLEQ 664
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778166 793 VEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLklqqQSMKALQDERE 850
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRV----EALEALYDEAE 718
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
603-879 |
4.57e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.44 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 603 LEHYKKIMIQSEELRAQVNAsLETQQSLQEEN--LAEKEKL-TEKLE-QEEKLKARIQQLTEEKAALEESVAEEKNKLQG 678
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINI-LEMRLSETDARikLAAQEKIhVEILEeQLEKLRNELLIRGATEGLCVHSLSKELDVLKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 679 DLEMTQARVHELENDLACQKEVLESSVTQEKRkmREVLEAERRkaqDLENQL-TQQKEISESNTYEKlkmrDTLEKEKRR 757
Cdd:PLN02939 234 ENMLLKDDIQFLKAELIEVAETEERVFKLEKE--RSLLDASLR---ELESKFiVAQEDVSKLSPLQY----DCWWEKVEN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 758 IQDLENRLTKQREEIELKGQKEDILNNKLKdalllvedaqqmrtaestraeklslKLKETLAELEITKakmiMAEDRLKL 837
Cdd:PLN02939 305 LQDLLDRATNQVEKAALVLDQNQDLRDKVD-------------------------KLEASLKEANVSK----FSSYKVEL 355
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958778166 838 QQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEE 879
Cdd:PLN02939 356 LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
19-96 |
4.86e-06 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 50.53 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 19 TIGKHEDSDLVLQSSD--IDNHHALIEFneAEGTFVLQDFNTrNGTFVNECHI---QNVAVKLIPGDILRFGSsgptYEL 93
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTDLST-NGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
...
gi 1958778166 94 VIE 96
Cdd:COG3456 102 RVE 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
652-866 |
4.92e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 652 KARIQQLTEEKAALEESVAEEKNKLQgDLEMTQARVHELENDLACQKEVLESSVtqekrkmrEVLEAERRkAQDLENQLT 731
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEI--------DVASAERE-IAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 732 QqkeISESNtyeklkmrDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQ-QMRTAESTRAEKL 810
Cdd:COG4913 679 R---LDASS--------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdRLEAAEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778166 811 SLKLKETLAELEITKAkmiMAEDRLKLQQQsMKALQDERESQKHGFEEEITEYKEQ 866
Cdd:COG4913 748 RALLEERFAAALGDAV---ERELRENLEER-IDALRARLNRAEEELERAMRAFNRE 799
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
11-87 |
6.24e-06 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 46.89 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 11 FFVLKKSTTIGKHEDSDLVLQSSD--IDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHIQNVAVKLIP-----GDILR 83
Cdd:cd22686 21 FIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELK 100
|
....
gi 1958778166 84 FGSS 87
Cdd:cd22686 101 IGET 104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
249-707 |
6.63e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 249 LQAEIADLSQRLSEMAAvvaaARQSNRcdpRFQDLDEGD----DHRQKEIESMKSQINALQKGYSQVLSQTLAERNTEIE 324
Cdd:pfam15921 379 LQKLLADLHKREKELSL----EKEQNK---RLWDRDTGNsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 325 SLKNEGENLKRDQAITSG------MVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKE--DLRKE 396
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQlestkeMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvDLKLQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 397 EAQKERREAQ-----EKELKLCRSQMQDMEKEVKKLREELKkNYTgqNVISKTLREKNKLENFRSQVikatfgktkpfrD 471
Cdd:pfam15921 532 ELQHLKNEGDhlrnvQTECEALKLQMAEKDKVIEILRQQIE-NMT--QLVGQHGRTAGAMQVEKAQL------------E 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 472 KPVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNVEKLRV----------LLDKCQACmRDSCNSMDLK 541
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAvkdikqerdqLLNEVKTS-RNELNSLSED 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 542 KEVELLQHLQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLniELSDSdkgfslcliylleHYKKIMIQseeLRAQVN 621
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM--EGSDG-------------HAMKVAMG---MQKQIT 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 622 ASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAaleeSVAEEKNKLQGDLEMTQARVHELENDLACQKEVL 701
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS----TVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
....*.
gi 1958778166 702 ESSVTQ 707
Cdd:pfam15921 814 DKASLQ 819
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
18-87 |
7.22e-06 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 46.07 E-value: 7.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778166 18 TTIGKHEDSDLVLQSSDIDNHHALIE---FNEAEGTFV-LQDfNTRNGTFVNECHI-QNVAVKLIPGDILRFGSS 87
Cdd:cd22670 24 ITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIAHS 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-671 |
9.55e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 317 AERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLR-------IQNKEKEYQLEALTSRCSKL 389
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 390 KEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQN----VISKTLREKNK-LENFRSQVIKATFG 464
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAeLTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 465 KTKPFRDKPVTDQQLI----------ERIVQVTEDNLSFQQRKWTLQRETHLHSKQ-EEVVHNVEKLRVLLDKCQACMRD 533
Cdd:TIGR02168 826 LESLERRIAATERRLEdleeqieelsEDIESLAAEIEELEELIEELESELEALLNErASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 534 SCNSM-DLKKEVELLQHlQLSPPVLGLQKAVLNILRVslswleeTEQLLGDLNIELSDsdkgfslcliyLLEHYKKIMIQ 612
Cdd:TIGR02168 906 LESKRsELRRELEELRE-KLAQLELRLEGLEVRIDNL-------QERLSEEYSLTLEE-----------AEALENKIEDD 966
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 613 SEELRAQVnASLETQ-QSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAE 671
Cdd:TIGR02168 967 EEEARRRL-KRLENKiKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
15-87 |
1.02e-05 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 45.48 E-value: 1.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778166 15 KKSTTIGKHEDSDLVLQSSDIDNHHALIEfnEAEGTFVLQDFNTRNGTFVNECHIQNVAVKliPGDILRFGSS 87
Cdd:cd22698 20 QDEFTIGRSSNNDIRLNDHSVSRHHARIV--RQGDKCNLTDLGSTNGTFLNGIRVGTHELK--HGDRIQLGET 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
649-897 |
1.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 649 EKLKARIQQLTEEKAALEEsvAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLEN 728
Cdd:COG4913 228 DALVEHFDDLERAHEALED--AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 729 QLTQQkeisesntyeklkmRDTLEKEKRRIQDLENRLTKQREEIelKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAE 808
Cdd:COG4913 306 RLEAE--------------LERLEARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 809 KLSLKLKETLAELEITKAkmimaedRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYY 888
Cdd:COG4913 370 ALGLPLPASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
....*....
gi 1958778166 889 RKIEGEIAT 897
Cdd:COG4913 443 LALRDALAE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
331-1026 |
1.52e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 331 ENLKRDQAITSGMVTSLQKdVSARNEQVQQLQEEVNQLRiqNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEKEL 410
Cdd:TIGR02168 186 ENLDRLEDILNELERQLKS-LERQAEKAERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 411 KLCRSQMQDMEKEVKKLREELKKNYTGQNVISKTLREKNKlenfRSQVIKATFgktkpfrdkpvtdQQLIERIVQVTEDN 490
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ----QKQILRERL-------------ANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 491 LSFQQRKWTLQRETHLHSKQEEVVH-NVEKLRVLLDKCQACMRDSCNSMDLKKEvellQHLQLSPPV--LGLQKAVLNil 567
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKeELESLEAELEELEAELEELESRLEELEE----QLETLRSKVaqLELQIASLN-- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 568 rvslSWLEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQ 647
Cdd:TIGR02168 400 ----NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 648 EE-KLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARvHELENDLACQKEVLE------------------------ 702
Cdd:TIGR02168 476 ALdAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ-SGLSGILGVLSELISvdegyeaaieaalggrlqavvven 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 703 --------SSVTQEKRKMREVLEAERRKAQDLENQLTQQKE------------ISESNTYEK--------LKMRDTLE-- 752
Cdd:TIGR02168 555 lnaakkaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKniegflgvakdlVKFDPKLRKalsyllggVLVVDDLDna 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 753 ----KEKRR----------------------------IQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMR 800
Cdd:TIGR02168 635 lelaKKLRPgyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 801 TAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQkhgfEEEITEYKEQIKQHSQTIVNLEER 880
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL----EERLEEAEEELAEAEAEIEELEAQ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 881 LSQvtqyyrkIEGEIATLKDSDSAQKEEVPQEftivpSLDSSAKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAH 960
Cdd:TIGR02168 791 IEQ-------LKEELKALREALDELRAELTLL-----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778166 961 TRMSDLRgELSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEK 1026
Cdd:TIGR02168 859 AEIEELE-ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
586-1333 |
1.67e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 586 IELSDSDKGFSLCLIYLLEHYKKIMIQSEElraqvnASLETQQSLQEENLAEKEKLTEKL-----------------EQE 648
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKK------ALEYYQLKEKLELEEEYLLYLDYLklneeridllqellrdeQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 649 EKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVT----------QEKRKMREVLEA 718
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVddeeklkeseKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 719 ERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEI----ELKGQKEDILNNKLKDALLLVE 794
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLssaaKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 795 DAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTI 874
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 875 VNLEERLSQVTQY---YRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIACDHLIDDLLMAQKEILSQQEIIMK 951
Cdd:pfam02463 493 QKLEERSQKESKArsgLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 952 LRTDLGEAHTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEKPRPYL 1031
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1032 STEQKPRNLSQKCDISLQIEPAHPDSFSSFQEEQffSDLGAKCKGSRHEEVIQRQKKALSELRTRIKELEKANSSNHKDH 1111
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKELLEIQELQEKAE--SELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1112 VNESFLELKTLRMEKNVQKILLDAkpdlttfSRVEIRPPLNGPFSSGSPFAMEKSMKTDAAEALELSEKLYTDMIKTLGS 1191
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEK-------SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1192 LMNIKDMSSHMSLKHLSPKERERVNHLRQKDLDLVFDKITQLKTRLQRKEELVRGYEWELEQLRHSKVSVQM--YQTQVA 1269
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKeeELEEQK 883
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958778166 1270 KLEDDIHKEAEEKALLKEALDRTEQQLSQEKRLNRAFKQQKDRVEDQEQRNSSCSCPFKENEKQ 1333
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
19-86 |
2.81e-05 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 44.17 E-value: 2.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778166 19 TIGKHEDSDLVLQSSDIDNHHALIEFnEAEGtFVLQDFNTRNGTFVNECHIQNVAVKLIPGDILRFGS 86
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEV-DDEG-WRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
17-87 |
3.37e-05 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 43.99 E-value: 3.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778166 17 STTIGKHEDSDLVLQSSDIDNHHALIEFNeaEGTFVLQDFNTRNGTFVNECHIQnVAVKLIPGDILRFGSS 87
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWD--GQVAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHS 86
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
586-807 |
3.89e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 586 IELSDSDKGFSL------------CLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEK-LTEKLEQEEKLK 652
Cdd:PRK05771 34 EDLKEELSNERLrklrslltklseALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKeIKELEEEISELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 653 ARIQQLTEEKAALE--ESVaEEKNKLQGDLEMTQARVHELENDLACQKEVLESS-----VTQEKRKMREVLEAERRKAQD 725
Cdd:PRK05771 114 NEIKELEQEIERLEpwGNF-DLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVenveyISTDKGYVYVVVVVLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 726 LENQLtQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQM--RTAE 803
Cdd:PRK05771 193 VEEEL-KKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEAlsKFLK 271
|
....
gi 1958778166 804 STRA 807
Cdd:PRK05771 272 TDKT 275
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
604-781 |
4.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 604 EHYKKIMIQSEELRAQVNA--------SLETQQSLQEENLAEKEKLTEKLEQeekLKARIQQLTEEKAALEESVAE---- 671
Cdd:COG4913 262 ERYAAARERLAELEYLRAAlrlwfaqrRLELLEAELEELRAELARLEAELER---LEARLDALREELDELEAQIRGnggd 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 672 EKNKLQGDLEMTQARVHELENDLACQKEVLEsSVTQEKRKMREVLEAERRKAQDLENQLTQQKEisesntyeklKMRDTL 751
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEELE----------ALEEAL 407
|
170 180 190
....*....|....*....|....*....|.
gi 1958778166 752 EKEKRRIQDLENRLTKQREEIE-LKGQKEDI 781
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIAsLERRKSNI 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
708-924 |
5.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 708 EKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIElkgQKEDILNNKLK 787
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE---ERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 788 ------------DALL-------LVEDAQQMRTAESTRAEKLSlKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDE 848
Cdd:COG3883 94 alyrsggsvsylDVLLgsesfsdFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778166 849 RESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAK 924
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
249-429 |
7.39e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 249 LQAEIADLSQRLSEMAAVVAAARQSNrcdpRFQDLDEGDDHRQKEIESMKSQINALQ------KGYSQVLSQTLAERNTE 322
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKN----GLVDLSEEAKLLLQQLSELESQLAEARaelaeaEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 323 IESLKNEGE--NLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQ-NKEKEYQLEALTSRCSKLKEDLRKEEAQ 399
Cdd:COG3206 256 LPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQ 335
|
170 180 190
....*....|....*....|....*....|
gi 1958778166 400 KERREAQEKELKLCRSQMQDMEKEVKKLRE 429
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
263-433 |
7.78e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 263 MAAVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNE----GENLKRDQA 338
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEiaeaEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 339 ITSGMVTSLQKDVSARNE-----QVQQLQEEVNQLRIQNKEKEYQLEALTSrcskLKEDLRKEEAQKERREAQEKELKLC 413
Cdd:COG3883 87 ELGERARALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEAL 162
|
170 180
....*....|....*....|
gi 1958778166 414 RSQMQDMEKEVKKLREELKK 433
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEA 182
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
291-772 |
9.11e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 291 QKEIESMKSQINALQKgysqvlsqtlaerntEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRI 370
Cdd:TIGR02169 680 RERLEGLKRELSSLQS---------------ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 371 QNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEKELK--LCRSQMQDMEKEVKKLREELKKnytgqnvISKTLREK 448
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKLEEEVSR-------IEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 449 NKLENFRSQvikatfgktkpfrdkpvtDQQLIERIVQvtedNLSFQQRKWTLQREthlhskqeevvhnveklrvlldkcq 528
Cdd:TIGR02169 818 EQKLNRLTL------------------EKEYLEKEIQ----ELQEQRIDLKEQIK------------------------- 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 529 acmrdscnsmDLKKEVELLQhlqlsppvlglqkavlnilrvslSWLEETEQLLGDLNIELSDsdkgfslcliyLLEHYKK 608
Cdd:TIGR02169 851 ----------SIEKEIENLN-----------------------GKKEELEEELEELEAALRD-----------LESRLGD 886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 609 IMIQSEELRAQvnasLETQQSLQEENLAEKEKLTEKLEQeekLKARIQQLTEEKAALEESVAEEknklqgdlemtqarvh 688
Cdd:TIGR02169 887 LKKERDELEAQ----LRELERKIEELEAQIEKKRKRLSE---LKAKLEALEEELSEIEDPKGED---------------- 943
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 689 elendlacQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQ 768
Cdd:TIGR02169 944 --------EEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
....
gi 1958778166 769 REEI 772
Cdd:TIGR02169 1016 KREV 1019
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
704-1100 |
9.39e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 704 SVTQEKRKMREVLEAERRKAQDLENQLT-QQKEISE------------SNTYEKLKMRDTLEKEKRRIQDLENRLTKQRE 770
Cdd:COG5022 804 SLLGSRKEYRSYLACIIKLQKTIKREKKlRETEEVEfslkaevliqkfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQ 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 771 EIELKGQKE------DILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQqsmka 844
Cdd:COG5022 884 LQELKIDVKsisslkLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNK----- 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 845 LQDERESQKhgfeEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIeGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAK 924
Cdd:COG5022 959 LHEVESKLK----ETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 925 eiacdhliddLLMAQKEILSQQEIIMKLRTDLGEA--HTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQT 1002
Cdd:COG5022 1034 ----------IISSESTELSILKPLQKLKGLLLLEnnQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1003 TGL-VEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLSQK--------------CDISLQIEPAHPDSFSSFQEEQFF 1067
Cdd:COG5022 1104 TNRnLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVfqklsvlqleldglFWEANLEALPSPPPFAALSEKRLY 1183
|
410 420 430
....*....|....*....|....*....|...
gi 1958778166 1068 SDLGAKCKGSRHEEVIQRQKKALSELRTRIKEL 1100
Cdd:COG5022 1184 QSALYDEKSKLSSSEVNDLKNELIALFSKIFSG 1216
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
209-458 |
9.40e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 209 MDQDLGQQDKDDiillLGREINRLSDFEMESKYKDAViMNLQAEIADLSQRLsemaavvaaARQSNRCDPRFQDLD---E 285
Cdd:pfam17380 296 MEQERLRQEKEE----KAREVERRRKLEEAEKARQAE-MDRQAAIYAEQERM---------AMERERELERIRQEErkrE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 286 GDDHRQKEIESMKSQINALQKgySQVLSQTLAER-NTEIESLKN----EGENLKRDQAITSGMVTSLQKDVSARNEQVQQ 360
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELER--LQMERQQKNERvRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 361 LQEE----VNQLRIQNKEKEYQLEAL--------TSRCSKLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLR 428
Cdd:pfam17380 440 LEEErareMERVRLEEQERQQQVERLrqqeeerkRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
250 260 270
....*....|....*....|....*....|
gi 1958778166 429 EELKKNytgQNVISKTLREKNKLENFRSQV 458
Cdd:pfam17380 520 KEMEER---QKAIYEEERRREAEEERRKQQ 546
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
317-788 |
9.55e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 317 AERNTEIESLKNEGENLKR-DQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRK 395
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 396 EEAQKERREAQEK----ELKLCRSQMQDMEKEVKKLREELKKnytgQNVISKTLREKNKLENFRSqviKATFGKTKPFRD 471
Cdd:PTZ00121 1378 KKADAAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAAKKK----ADEAKKKAEEKKKADEAKK---KAEEAKKADEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 472 KPVTDQQLIERIVQVTEDNLSFQQRKWTLQ---RETHLHSKQEEVVHNVEKLRV----------LLDKCQACMRDSCNSM 538
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEeakKADEAKKKAEEAKKKADEAKKaaeakkkadeAKKAEEAKKADEAKKA 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 539 DLKKEVELLQHLQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLNI------ELSDSDKGFSLCLIYLLEHYKKImiQ 612
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMalrkaeEAKKAEEARIEEVMKLYEEEKKM--K 1608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 613 SEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKA----------RIQQLTEEKAALEESVAEEKNKLQGDLEM 682
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 683 TQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLENqlTQQKEISESNTYEKLKMRdtlEKEKRRIQDLE 762
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE--AKKEAEEDKKKAEEAKKD---EEEKKKIAHLK 1763
|
490 500
....*....|....*....|....*.
gi 1958778166 763 NRLTKQREEIelKGQKEDILNNKLKD 788
Cdd:PTZ00121 1764 KEEEKKAEEI--RKEKEAVIEEELDE 1787
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
625-774 |
1.24e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.48 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 625 ETQQSLQEENLAEKEKLTEKLEQE-----EKLKARIQQLTEEKAALEESvaEEKNKLQgdLEMTQARVHELENDLACQKE 699
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEEE--ERKQRLQ--LQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778166 700 VLESSVTQEKrkmREVLEAERRKAQDLENQLT-QQKEISESNTYEKLK-MRDTLEKEKRRIQDLENRLTKQREEIEL 774
Cdd:pfam15709 434 ELQRKKQQEE---AERAEAEKQRQKELEMQLAeEQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARL 507
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
38-85 |
1.33e-04 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 43.03 E-value: 1.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958778166 38 HHALIEFNEaeGTFVLQDFNTRNGTFVNECHIQ-----NVAVKLIPGDILRFG 85
Cdd:cd22679 52 NHALLWYDD--GKFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDIVQFG 102
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
604-1105 |
1.35e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 604 EHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEE--SVAEEKNKLQGDLE 681
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllSNLKKKIQKNKSLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 682 mtqARVHELENdlacQKEVLESSVTQEKRKMREvLEAERRKAQDLENQLTQQKEISESNTYEKLKmrdTLEKEKRRIQDL 761
Cdd:TIGR04523 218 ---SQISELKK----QNNQLKDNIEKKQQEINE-KTTEISNTQTQLNQLKDEQNKIKKQLSEKQK---ELEQNNKKIKEL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 762 ENRLTKQREEIE-LKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEitKAKMIMAEDRLKLQQQ 840
Cdd:TIGR04523 287 EKQLNQLKSEISdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK--KELTNSESENSEKQRE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 841 smkalQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKdsdsAQKEEVPQEFTIVPSLD 920
Cdd:TIGR04523 365 -----LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEKEIERLKETI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 921 SSAKEIacdhlIDDLlmaQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELsEKQKTELERQVALVRQQNSELSILKAKVV 1000
Cdd:TIGR04523 436 IKNNSE-----IKDL---TNQDSVKELIIKNLDNTRESLETQLKVLSRSI-NKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1001 QttglVEKKDRELKVLREALRASQEKprpyLSTE--QKPRNLSQKCDISLQIEpahpdsfssfqeeqffSDLgakcKGSR 1078
Cdd:TIGR04523 507 E----LEEKVKDLTKKISSLKEKIEK----LESEkkEKESKISDLEDELNKDD----------------FEL----KKEN 558
|
490 500
....*....|....*....|....*..
gi 1958778166 1079 HEEVIQRQKKALSELRTRIKELEKANS 1105
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
313-771 |
1.46e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.27 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 313 SQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEd 392
Cdd:pfam05557 96 ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 393 LRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISKTLREKN-------KLENFRSQVIKATFGK 465
Cdd:pfam05557 175 LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEdlkrkleREEKYREEAATLELEK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 466 TKPFRD-------------KPVTDQQLIERIVQVTEDNLSFQQRKWTLQRET-HLHSKQEEVVHnveKLRVLLDKCQacm 531
Cdd:pfam05557 255 EKLEQElqswvklaqdtglNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSArQLEKARRELEQ---ELAQYLKKIE--- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 532 rdscnsmDLKKEVELLQHLqlsppVLGLQKAVLNILRVSLSWLEETEQLLGDLNieLSDSDKGFSLCLIYLLEHYKKIMI 611
Cdd:pfam05557 329 -------DLNKKLKRHKAL-----VRRLQRRVLLLTKERDGYRAILESYDKELT--MSNYSPQLLERIEEAEDMTQKMQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 612 QSEELRAQVNASLET-------------------QQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVaeE 672
Cdd:pfam05557 395 HNEEMEAQLSVAEEElggykqqaqtlerelqalrQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMEL--E 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 673 KNKLQGDLEMTQARVHELENDLACQKEvlessvtQEKRKMREVLEAE--------RRKAQDLENQLTQQKEISESNTYEK 744
Cdd:pfam05557 473 RRCLQGDYDPKKTKVLHLSMNPAAEAY-------QQRKNQLEKLQAEierlkrllKKLEDDLEQVLRLPETTSTMNFKEV 545
|
490 500
....*....|....*....|....*..
gi 1958778166 745 LKMRDTLEKEKRRIQDLENRLTKQREE 771
Cdd:pfam05557 546 LDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
11-91 |
1.53e-04 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 42.31 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALI-----EFNEAEG----TFVLQDFNtRNGTFVNECHIQNVA-VKLIPGD 80
Cdd:cd22667 15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvlhpEANLSDPdtrpELTLKDLS-KYGTFVNGEKLKGGSeVTLKDGD 93
|
90
....*....|.
gi 1958778166 81 ILRFGSSGPTY 91
Cdd:cd22667 94 VITFGVLGSKF 104
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
712-908 |
1.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 712 MREVLEAE-RRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIE-LKGQKEDILN--NKLK 787
Cdd:COG4717 43 IRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEeLEAELEELREelEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 788 DALLLVEDAQQMRTAESTRAEKLSL--KLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKhgfEEEITEYKE 865
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT---EEELQDLAE 199
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958778166 866 QIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEE 908
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
318-1024 |
1.96e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 318 ERNTEIE-SLKNEGENLKRDQAITSGMVTSLQKDVSarnEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKE 396
Cdd:TIGR00606 383 ERGPFSErQIKNFHTLVIERQEDEAKTAAQLCADLQ---SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 397 EAQKERREAQEKELklcrsqmQDMEKEVKKLREELKKNYTGQNVISKTLREKNkLENFRSQVIKA--------------- 461
Cdd:TIGR00606 460 IKELQQLEGSSDRI-------LELDQELRKAERELSKAEKNSLTETLKKEVKS-LQNEKADLDRKlrkldqemeqlnhht 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 462 -TFGKTKPFRDKPVTDQQLIERIVQVTEDNLSFQ--QRKWTLQRETHLHSKQEEVVHNVEKLRVLLDKCQAC--MRDSCN 536
Cdd:TIGR00606 532 tTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLeqNKNHIN 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 537 SMDLKKEVELLQHLQLSPPVLGLQKAVLNILRVSLSWLEETEQL--------LGDLNIELSdSDKGFSLCLIYllehykK 608
Cdd:TIGR00606 612 NELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRamlagataVYSQFITQL-TDENQSCCPVC------Q 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 609 IMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLkarIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVH 688
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDE---MLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 689 ELENDLACQKEVLESSVTQEKRK---MREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKrriQDLENRL 765
Cdd:TIGR00606 762 RLKNDIEEQETLLGTIMPEEESAkvcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK---QEKQHEL 838
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 766 TKQREEIEL-----KGQKEDILN-----NKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRL 835
Cdd:TIGR00606 839 DTVVSKIELnrkliQDQQEQIQHlksktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL 918
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 836 KLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRK-----IEGEIATLKDSDSAQKEEVP 910
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqketeLNTVNAQLEECEKHQEKINE 998
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 911 QEFTIVPSLDSSAKeiacdhliddllmaQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELSEKQKTELERQvalVRQQNS 990
Cdd:TIGR00606 999 DMRLMRQDIDTQKI--------------QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQE---HQKLEE 1061
|
730 740 750
....*....|....*....|....*....|....
gi 1958778166 991 ELSILKAKVVQTTGLVEKKDRELKVLREALRASQ 1024
Cdd:TIGR00606 1062 NIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
637-1382 |
2.02e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 637 EKEKLTEKLEQE-EKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRKMREV 715
Cdd:pfam02463 170 KKKEALKKLIEEtENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 716 LEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLvED 795
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA-EK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 796 AQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIV 875
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 876 NLEERLSQV-------TQYYRKIEGEIATLKDSDSAQKEEVpQEFTIVPSLDSSAKEIACDHLIDDLLMAQKEILSQQEI 948
Cdd:pfam02463 409 LLLELARQLedllkeeKKEELEILEEEEESIELKQGKLTEE-KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 949 IMKLRTDLGEAHTRMSDLRGELSEKQK--------TELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREAL 1020
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLAlikdgvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1021 RASQEKPRPYLSTEQKPR-----NLSQKCDISLQIEPAHPDSFSSFQEEQFFSDLGAKCKGSRHEEVIQRQ--KKALSEL 1093
Cdd:pfam02463 568 RALTELPLGARKLRLLIPklklpLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesAKAKESG 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1094 RTRIKELEKANSSNHKDHVNESFLELKTLRMEKNVQKILLDAKPdLTTFSRVEIRPPLNGPFSSGSPFAMEKSMKTDAAE 1173
Cdd:pfam02463 648 LRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK-EEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1174 ALELSEKLYTDMIKTLGSLMNIKDMSSHMSLKHLSPKERERVNHLRQKDLDLVFDKITQLKTRLQRKEELVRGYEWELEQ 1253
Cdd:pfam02463 727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1254 LRHSKVSVQMY---QTQVAKLEDDIHKEAEEKALLKEALDRTEQQLSQEKRLNRAFKQQKDRVEDQEQRNSSCSCPFKEN 1330
Cdd:pfam02463 807 EEELKEEAELLeeeQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKD 886
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1958778166 1331 EKQRRIFVEMVKRKMQDSSLQAGAKKATLKTGQERETKKEACKPTQSLSFIK 1382
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
390-1245 |
2.35e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 390 KEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKnytgqnvisktLREKNKLENFRSQVIKATFGKTKpf 469
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA-----------LEYYQLKEKLELEEEYLLYLDYL-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 470 rdkpvtdQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNVEKLRVLLDKCQACMRDSCNSMDLKKEVELLQH 549
Cdd:pfam02463 233 -------KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 550 LQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKimiqSEELRAQVNASLETQQS 629
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL----QEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 630 LQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEK 709
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 710 RKMREVLEAER-RKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILN----- 783
Cdd:pfam02463 462 KDELELKKSEDlLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVaveny 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 784 ---NKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEI 860
Cdd:pfam02463 542 kvaISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 861 TEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVpQEFTIVPSLDSSAKEIACDHLIDDLLMAQK 940
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSE-LTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 941 EILSQQEIIMKLRTDLGEAHTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKvvqttGLVEKKDRELKVLREAL 1020
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-----KEEKEEEKSELSLKEKE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1021 RASQEKPRPYLSTEQKPRNLSQKCDISLQIEPAHPDSFSSFQEEqffSDLGAKCKGSRHEEVIQRQKKALSELRTRIKEL 1100
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE---EQLLIEQEEKIKEEELEELALELKEEQKLEKLA 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1101 EKANSSNHKDHVNESFLELKTLRMEKNVQKILLDAKPDLTTFSRVEIRPPLNGPFSSGSPFAMEKSMKTDAAEALELSEK 1180
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778166 1181 L--YTDMIKTLGSLMNIKDMSSHMSLKHLSPKERERVNHLRQKDLDLVFDKITQLKTRLQRKEELVR 1245
Cdd:pfam02463 933 YeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
603-1020 |
2.44e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 603 LEHYKKIMIQSEELRAQVNASLETQQSLQEEN-----LAEKE-KLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKL 676
Cdd:PRK01156 321 INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNnqileLEGYEmDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 677 QGDLEMTQARVHELENDLAcQKEVLESSVTQEKRKMREVLEAERRKAQDLENQ---------LTQQK--EISESNTYEKL 745
Cdd:PRK01156 401 EIDPDAIKKELNEINVKLQ-DISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKsnHIINHYNEKKS 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 746 KMRDTLEKEKRRIQDLENRLT--KQREEIELKGQKEDILN--NKLKDALLLVEDaqqMRTAESTraeklsLKLKETLAEL 821
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVdlKKRKEYLESEEINKSINeyNKIESARADLED---IKIKINE------LKDKHDKYEE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 822 EITKAKMIMAEDRLKLQQQSMKALQD----ERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIAT 897
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANN 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 898 LKDSDSAQKEEVPQEFTIVPSLDSSAKEIAcdhLIDDLLMAQKEILSQqeiIMKLRTDLGEAHTRMSDLRGELSEKQKTe 977
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKIDNYKKQIA---EIDSIIPDLKEITSR---INDIEDNLKKSRKALDDAKANRARLEST- 703
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958778166 978 lerqVALVRQQNSELSILKA---KVVQTTGLVEKKDRELKVLREAL 1020
Cdd:PRK01156 704 ----IEILRTRINELSDRINdinETLESMKKIKKAIGDLKRLREAF 745
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
225-433 |
2.74e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 225 LGREIN----RLSDFEMESKYKDAVIMNLQAEIADLSQrlsEMAAVVAAARQSNRCdprFQDLDEGDDHRQKEIESMKSQ 300
Cdd:pfam15921 595 LEKEINdrrlELQEFKILKDKKDAKIRELEARVSDLEL---EKVKLVNAGSERLRA---VKDIKQERDQLLNEVKTSRNE 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 301 INALQKGY-----------------SQVLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQE 363
Cdd:pfam15921 669 LNSLSEDYevlkrnfrnkseemettTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS 748
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958778166 364 EVNQLRI----QNKEKEYqleaLTSRCSKLKEDLRKEEAQKERREAqekELKLCRSQMQDMEKEVKKLREELKK 433
Cdd:pfam15921 749 KIQFLEEamtnANKEKHF----LKEEKNKLSQELSTVATEKNKMAG---ELEVLRSQERRLKEKVANMEVALDK 815
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
744-1033 |
2.76e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 744 KLKMRDTLEKEKRRIQDLE---NRLTKQREEIElkgqkedilnNKLKDALLLVEDAQQMRTAESTRAEKLslklketlaE 820
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKrelSSLQSELRRIE----------NRLDELSQELSDASRKIGEIEKEIEQL---------E 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 821 LEITKAKMIMAEDRLKLQQQSMKALQDERESQKhgFEEEITEYKEQIKQHSQTIVNLEERLSQvtQYYRKIEGEIatlkd 900
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKE--LEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAEL----- 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 901 sdSAQKEEVPQEFTIVPSLDSSAKEiacdhLIDDLLMAQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELsEKQKTELER 980
Cdd:TIGR02169 801 --SKLEEEVSRIEARLREIEQKLNR-----LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK-EELEEELEE 872
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958778166 981 QVALVRQQNSELSILKAKVVQttglVEKKDRELKVLREALRASQEKPRPYLST 1033
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
11-65 |
2.88e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438772 [Multi-domain] Cd Length: 100 Bit Score: 41.53 E-value: 2.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958778166 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHAliEFNEAEGTFVLQDFNTRNGTFVN 65
Cdd:cd22720 19 FLLDQAITSAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVN 71
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
636-923 |
2.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 636 AEKEKLTEKLEQEEKLKARIQQLTEEKAALEEsvaeEKNKLQGDLEMTQARVHELENDLAcqkeVLESSVTQEKRKMREV 715
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKLQAEIA----EAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 716 LEAerrkaqdlenqltQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIElkgqkedilnnKLKDALLLVED 795
Cdd:COG3883 92 ARA-------------LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLE-----------ELKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 796 AQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIV 875
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958778166 876 NLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSA 923
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| FHA_OdhI-like |
cd22721 |
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ... |
11-65 |
3.17e-04 |
|
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI) and similar proteins; OdhI is an essential component of the PknG signaling pathway. It regulates glutamate production under biotin non-limiting conditions. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438773 [Multi-domain] Cd Length: 102 Bit Score: 41.61 E-value: 3.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958778166 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHAliEFNEAEGTFVLQDFNTRNGTFVN 65
Cdd:cd22721 24 FLLDQPTTTAGRHPESDIFLDDVTVSRRHA--EFRINEGEFEVVDVGSLNGTYVN 76
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
705-999 |
3.65e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 705 VTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTY----EKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKED 780
Cdd:PTZ00440 1075 IKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVnadkEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDI 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 781 ILNN----KLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMImAEDRLKLQQQSMKALQDERESQKHGF 856
Cdd:PTZ00440 1155 TLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMS-KERNDHLTTFEYNAYYDKATASYENI 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 857 EEEITEYK--EQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEvpQEFTIVPSLDSSAKEI--ACDHLI 932
Cdd:PTZ00440 1234 EELTTEAKglKGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNM--YEFLISIDSEKILKEIlnSTKKAE 1311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778166 933 DDLLMAQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELSEKQkteLERQVALVRQQNSELSILKAKV 999
Cdd:PTZ00440 1312 EFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEDKQ---IDDEIKKIEQIKEEISNKRKEI 1375
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
612-1054 |
4.24e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 612 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARI------QQLTEEKAALEESVAEEKNKLQGDLEMTQA 685
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrealqqTQQSHAYLTQKREAQEEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 686 RVHELENDLAcQKEVLESSVTQEKRKMREVLEAER----RKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDL 761
Cdd:TIGR00618 268 RIEELRAQEA-VLEETQERINRARKAAPLAAHIKAvtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 762 ENRLTKQREEIELKGQKEDILNNKLKDALLLVED--AQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQ 839
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 840 QSMKA---LQDERESQKHGFEEEITEYKEQIKQH----SQTIVNLEERLSQVTQYYRKiEGEIATLKDSDSAQKEEVPQE 912
Cdd:TIGR00618 427 AHAKKqqeLQQRYAELCAAAITCTAQCEKLEKIHlqesAQSLKEREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCP 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 913 F---------TIVPSLDSSAKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDlgeahtrmsdlRGELSEKQKTELERQVA 983
Cdd:TIGR00618 506 LcgscihpnpARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-----------RASLKEQMQEIQQSFSI 574
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958778166 984 LVRQQNS---ELSILKAKVVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTEQKpRNLSQKCDISLQIEPAH 1054
Cdd:TIGR00618 575 LTQCDNRskeDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV-RLHLQQCSQELALKLTA 647
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
290-485 |
4.51e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 290 RQKEIESMKSQINALQKgysqvlsqTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLR 369
Cdd:COG4942 25 AEAELEQLQQEIAELEK--------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 370 IQNKEKEYQLEAL------TSRCSKLKEDLRKE----------------EAQKERREAQEKELKLCRSQMQDMEKEVKKL 427
Cdd:COG4942 97 AELEAQKEELAELlralyrLGRQPPLALLLSPEdfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778166 428 REELKKNYTGQNVISKTLREKNKLENFRSQVIKATFGKTKPFRDKPVTDQQLIERIVQ 485
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
4-85 |
4.72e-04 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 40.79 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 4 YLKSPDgfFVLKK------STTIGKHEDSDLVLQSSDIDNHHALIEFNEaeGTFVLQDFNTRNGTFVNECHIQNVAVKLI 77
Cdd:cd22680 5 ILSSPN--LTGKKfpfdfsSVSIGRDPENVIVIPDPFVSRNHARITVDS--NEIYIEDLGSTNGTFVNDFKRIKGPAKLH 80
|
....*...
gi 1958778166 78 PGDILRFG 85
Cdd:cd22680 81 PNDIIKLG 88
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
222-434 |
4.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 222 ILLLGREINRLSDFEMESKYKDAVIMNLQAEIADLSQRLSEMAavvaaarqsnrcdprFQDLDEgDDHRQKEIESMKSQI 301
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG---------------FESVEE-LEERLKELEPFYNEY 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 302 NALQKGYSQvlsqtLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARN-----EQVQQLQEEVNQLRIQNKEKE 376
Cdd:PRK03918 605 LELKDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLR 679
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778166 377 YQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKL---CRSQMQDMEKEVKKLREELKKN 434
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlekALERVEELREKVKKYKALLKER 740
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
572-685 |
4.98e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.67 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 572 SWLEETEQLLGDLNIELSDSDKGFSLC---LIYLLEHYKKIMIQSEELRAQVNASLETQQSL----QEENLAEKEKLTEK 644
Cdd:pfam05911 716 SQLQESEQLIAELRSELASLKESNSLAetqLKCMAESYEDLETRLTELEAELNELRQKFEALevelEEEKNCHEELEAKC 795
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958778166 645 LEQEEKLkariqQLTEEKAALEESVAEEKNKLQGDLEMTQA 685
Cdd:pfam05911 796 LELQEQL-----ERNEKKESSNCDADQEDKKLQQEKEITAA 831
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-457 |
5.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 249 LQAEIADLSQRLSEMAAVVAAARQsnrcdpRFQDLDEGDDHRQKEIESMKSQINALQkgysqvLSQTLAERNTEIESLKN 328
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEA------ELDALQERREALQRLAEYSWDEIDVAS------AEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 329 egenlkrdqaiTSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLrkEEAQKERREAQEK 408
Cdd:COG4913 683 -----------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958778166 409 ELKLcRSQMQDMEKEVKKLREELKKNYTGQNviSKTLREKNKLENFRSQ 457
Cdd:COG4913 750 LLEE-RFAAALGDAVERELRENLEERIDALR--ARLNRAEEELERAMRA 795
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
612-724 |
5.79e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 612 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIqqlteEKAALEESVAEEKNKLQGDLEMtQARVHELE 691
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET-----ARAEAEAAYEIAEANAEREVQR-QLEIAERE 289
|
90 100 110
....*....|....*....|....*....|...
gi 1958778166 692 NDLACQKEVLESSVTQEKRKMREVLEAERRKAQ 724
Cdd:COG2268 290 REIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
15-86 |
5.99e-04 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 41.26 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 15 KKSTTIGK--HEDSD---LVLQSSDIDNHHALIEFNEaeGTFVLQDFNTRNGTFVNECHIQ------NVAVKLIPGDILR 83
Cdd:cd22702 31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKN--GAFFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
...
gi 1958778166 84 FGS 86
Cdd:cd22702 109 FGS 111
|
|
| PLN02829 |
PLN02829 |
Probable galacturonosyltransferase |
557-760 |
6.18e-04 |
|
Probable galacturonosyltransferase
Pssm-ID: 215443 [Multi-domain] Cd Length: 639 Bit Score: 44.07 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 557 LGLQKAVLNIL-RVSLSWLEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKIMIQSEE-LRAQVNASLE--TQQSLQE 632
Cdd:PLN02829 49 LGGDASKLNVLpQESSSSLKEPIGIVYSDNSSKTIEPDSQDLLLDKRGEHKARVLSATDDdTHSQTDDIIKqvTQKAGQD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 633 ENLAEKEKLTEKLEQEEKLKARIQQ--LTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKR 710
Cdd:PLN02829 129 DSDQQEKNSQSQSASQAESLEHVQQsaQTSEKVDEKEPLLTKTDKQTDQTVMPDARVRQLRDQLIKAKVYLSLPATKANP 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958778166 711 KMREVLEAERRKAQDLENQLTQQKEISEsNTYEKLK-MRDTLEKEKrRIQD 760
Cdd:PLN02829 209 HFTRELRLRIKEVQRVLGDASKDSDLPK-NANEKLKaMEQTLAKGK-QMQD 257
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
329-770 |
6.21e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 329 EGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEvnQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAqkeRREAQEK 408
Cdd:pfam07111 116 EAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQE--QLSSLTQAHEEALSSLTSKAEGLEKSLNSLET---KRAGEAK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 409 ELKLCRSQMQDMEKEVKKLREELK---------KNYTGQNVISKTLREKNKLENfrsqvikatfgktkpfrdkpvtdQQL 479
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEaqvtlveslRKYVGEQVPPEVHSQTWELER-----------------------QEL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 480 IERIVQVTEDNLSFQQRKWTLQRE----THLHSKQ-EEVVHNVEKLRVL----LDKCQACM---RDSCNSMDLKKEVELL 547
Cdd:pfam07111 248 LDTMQHLQEDRADLQATVELLQVRvqslTHMLALQeEELTRKIQPSDSLepefPKKCRSLLnrwREKVFALMVQLKAQDL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 548 QHL----QLSPPVLGLQKAVLN------ILRVSL----SWLEETEQLLGDLNIELSDSDKGFSlcliyllEHYKKIMIQS 613
Cdd:pfam07111 328 EHRdsvkQLRGQVAELQEQVTSqsqeqaILQRALqdkaAEVEVERMSAKGLQMELSRAQEARR-------RQQQQTASAE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 614 EELRAQVNASLETQQSLQ------EENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEE------SVAEEKNKLQGDLE 681
Cdd:pfam07111 401 EQLKFVVNAMSSTQIWLEttmtrvEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQlrqescPPPPPAPPVDADLS 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 682 MTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRK----AQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRR 757
Cdd:pfam07111 481 LELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQlsevAQQLEQELQRAQESLASVGQQLEVARQGQQESTEE 560
|
490
....*....|...
gi 1958778166 758 IQDLENRLTKQRE 770
Cdd:pfam07111 561 AASLRQELTQQQE 573
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
612-809 |
6.92e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 612 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQgdleMTQARVHELE 691
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY----RSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 692 --------NDLACQKEVLESSVTQEKRKMREvLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLEN 763
Cdd:COG3883 107 vllgsesfSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958778166 764 RLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEK 809
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
625-883 |
8.31e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 625 ETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEEsvaeeknKLQGDLEMTqARVHELENDLACQKEVLEss 704
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE-------QLQAETELC-AEAEEMRARLAARKQELE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 705 vtqekrkmrEVLeaerrkaQDLENQLTQQKEISESNTYEKLKMrdtlekeKRRIQDLENRLTKQ---REEIELKGQKEDI 781
Cdd:pfam01576 75 ---------EIL-------HELESRLEEEEERSQQLQNEKKKM-------QQHIQDLEEQLDEEeaaRQKLQLEKVTTEA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 782 LNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEiTKAKMImaeDRLKLQQQSMKALQDER-----------E 850
Cdd:pfam01576 132 KIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEE-EKAKSL---SKLKNKHEAMISDLEERlkkeekgrqelE 207
|
250 260 270
....*....|....*....|....*....|...
gi 1958778166 851 SQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQ 883
Cdd:pfam01576 208 KAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
230-405 |
1.27e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 230 NRLSDFEMESKYKDAVIMNLQAEIADLSQRLSE----MAAVVAAARQSNRCDP---------------RFQDLDEGDDHR 290
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIAELRAELEAqkeeLAELLRALYRLGRQPPlalllspedfldavrRLQYLKYLAPAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 291 QKEIESMKSQINALQKgysqvLSQTLAERNTEIESLKNEGENLKRdqaitsgmvtSLQKDVSARNEQVQQLQEEVNQLRI 370
Cdd:COG4942 149 REQAEELRADLAELAA-----LRAELEAERAELEALLAELEEERA----------ALEALKAERQKLLARLEKELAELAA 213
|
170 180 190
....*....|....*....|....*....|....*
gi 1958778166 371 QNKEKEYQLEALTsrcsKLKEDLRKEEAQKERREA 405
Cdd:COG4942 214 ELAELQQEAEELE----ALIARLEAEAAAAAERTP 244
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
15-85 |
1.31e-03 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 39.65 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778166 15 KKSTTIGKHEDSDLVLQSSD---IDNHHALIEFNeAEGTFVLQDFNTRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22663 20 GKEVTVGRGLGVTYQLVSTCplmISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
282-926 |
1.42e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 282 DLDEGDDHRQKEIESMKSQINALQKGYsQVLSQTLAERNTEIESLKNEGENLKRDQaitsgmvtslqKDVSARNEQVQQL 361
Cdd:PRK01156 142 SLISGDPAQRKKILDEILEINSLERNY-DKLKDVIDMLRAEISNIDYLEEKLKSSN-----------LELENIKKQIADD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 362 QEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLR---EELKK----- 433
Cdd:PRK01156 210 EKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKeleERHMKiindp 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 434 NYTGQNVISKTLREKNKLENFRsQVIKATFGKTKPFRDkpvtdqqLIERIVQVTEDNLSFQQRKwtlqrethlhSKQEEV 513
Cdd:PRK01156 290 VYKNRNYINDYFKYKNDIENKK-QILSNIDAEINKYHA-------IIKKLSVLQKDYNDYIKKK----------SRYDDL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 514 VHNVEKLRVLLDKCQACMRdscNSMDLKKevellqhlqlsppvlglqkavlnilrvslsWLEETEQLLGDLNIELSDSDK 593
Cdd:PRK01156 352 NNQILELEGYEMDYNSYLK---SIESLKK------------------------------KIEEYSKNIERMSAFISEILK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 594 GFSLCLIYLLEHYKKIMIQSEELRAQVnASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAA-LEESVAEE 672
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKV-SSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNhIINHYNEK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 673 KNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRKmrevLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLE 752
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINK----SINEYNKIESARADLEDIKIKINELKDKHDKYEEIKN 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 753 KEKR-RIQDLENRLTK------QREEIE---LKGQKEDIlNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELE 822
Cdd:PRK01156 554 RYKSlKLEDLDSKRTSwlnalaVISLIDietNRSRSNEI-KKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 823 ITKAKMimaedrlklqqQSMKALQDERESQKHGFEEEITEYKEQIKQHSQtivnLEERLSQVTQYYRKIEGEIATLKDSD 902
Cdd:PRK01156 633 NKYNEI-----------QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE----ITSRINDIEDNLKKSRKALDDAKANR 697
|
650 660
....*....|....*....|....
gi 1958778166 903 SAQKEEVPQEFTIVPSLDSSAKEI 926
Cdd:PRK01156 698 ARLESTIEILRTRINELSDRINDI 721
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
281-434 |
1.44e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 281 QDLDEGDDHRQKEIESMKSQINALQKGYSQV------LSQTLAERNTEIESLKNEGENLKRDQAITSGMV---------- 344
Cdd:pfam05667 324 ETEEELQQQREEELEELQEQLEDLESSIQELekeikkLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaeeni 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 345 TSLQKDVSARNEQVQQLQEEVNQLRIQNKEKeyqLEALTSRCSKlkedlRKEEAQKerreaQEKELKLCRSQMQDMEKEV 424
Cdd:pfam05667 404 AKLQALVDASAQRLVELAGQWEKHRVPLIEE---YRALKEAKSN-----KEDESQR-----KLEEIKELREKIKEVAEEA 470
|
170
....*....|
gi 1958778166 425 KKlREELKKN 434
Cdd:pfam05667 471 KQ-KEELYKQ 479
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
246-525 |
1.46e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 246 IMNLQAEIADLSQRLSEMA-AVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKgysqvlsqtlaERNTEIE 324
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKeRVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDR-----------ERLEELE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 325 SLKNEGENLKRDqaitsgmVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERRE 404
Cdd:pfam10174 472 SLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 405 AQEKELKLC---RSQMQDMEKEVKKLREELKKNYTGQNVISKTLR----EKN----KLENFRSQVIKATFGKTKPFRDKP 473
Cdd:pfam10174 545 NAEEAVRTNpeiNDRIRLLEQEVARYKEESGKAQAEVERLLGILRevenEKNdkdkKIAELESLTLRQMKEQNKKVANIK 624
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958778166 474 VTDQQLIERIVQVTEDNLsfqqRKWTLQRETHLHSKQEEVVHNVEKLRVLLD 525
Cdd:pfam10174 625 HGQQEMKKKGAQLLEEAR----RREDNLADNSQQLQLEELMGALEKTRQELD 672
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
11-85 |
1.70e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 39.53 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 11 FFVLKKSTTIGK---------HEDSDLVLQSSD-IDNHHALIEFNEAEGTFVLQDFNtRNGTFVNE--CHIQNVAVKLIP 78
Cdd:cd22701 12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVLG-RNGVKVDGilVKPGSPPVPLRS 90
|
....*..
gi 1958778166 79 GDILRFG 85
Cdd:cd22701 91 GSLIQIG 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
813-1028 |
1.82e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 813 KLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQkhgfEEEITEYKEQIKQHSQTIVNLEERLSQVTQyyrkie 892
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEK------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 893 gEIATLKDSDSAQKEEVPQ------------EFTIVPSLDSSAKEIACDHLIDDLLMAQKEIL----SQQEIIMKLRTDL 956
Cdd:COG4942 91 -EIAELRAELEAQKEELAEllralyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAeelrADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958778166 957 GEAHTRMSDLRGELsEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEKPR 1028
Cdd:COG4942 170 EAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
250-433 |
1.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 250 QAEIADLSQRLSEMAAVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQVLSQTLAERNTEIESLKNE 329
Cdd:COG4913 267 ARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 330 GENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQ-EK 408
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRElEA 426
|
170 180
....*....|....*....|....*
gi 1958778166 409 ELKLCRSQMQDMEKEVKKLREELKK 433
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAE 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
230-383 |
1.85e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 230 NRLSDFEMESKykdavIMNLQAEIADLSQRLSEMAAVVAAAR-QSNRCDPRFQDLDE---------GDDHRQKEIESMKS 299
Cdd:COG3206 196 AALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRAqlgsgpdalPELLQSPVIQQLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 300 QINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRD-QAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNK---EK 375
Cdd:COG3206 271 QLAELEAELAE-LSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAelpEL 349
|
....*...
gi 1958778166 376 EYQLEALT 383
Cdd:COG3206 350 EAELRRLE 357
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
345-432 |
2.68e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 345 TSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEyqLEALTSRCSKLKEDLRkeeAQKERREAQEKELKLCRSQMQDMEKEV 424
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQELQDLGVPADSGA--EERARARRDELHARLS---ANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
....*...
gi 1958778166 425 KKLREELK 432
Cdd:PRK04863 1098 RKLERDYH 1105
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
630-901 |
3.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 630 LQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEEsvAEEKNKLQGDLEMTQARVHELENDLAcqkEVLESSvtQEK 709
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQR--LAEYSWDEIDVASAEREIAELEAELE---RLDASS--DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 710 RKMREVLEAERRKAQDLENQLTQQKEIsesntyeklkmRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDI--LNNKLK 787
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGE-----------IGRLEKELEQAEEELDELQDRLEAAEDLARLELRalLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 788 DALL------LVEDAQQMRTAESTRAEKLSLKLKETLAELeitKAKMIMAEDRLKLQQQSMKALQDERESQKhgfEEEIT 861
Cdd:COG4913 757 AALGdavereLRENLEERIDALRARLNRAEEELERAMRAF---NREWPAETADLDADLESLPEYLALLDRLE---EDGLP 830
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958778166 862 EYKEQIKQ--HSQTIVNLEERLSQVTQYYRKIEGEIATLKDS 901
Cdd:COG4913 831 EYEERFKEllNENSIEFVADLLSKLRRAIREIKERIDPLNDS 872
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
348-453 |
3.15e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 348 QKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLrkeEAQKERREAQEKELKlcrsqmQDMEKEVKKL 427
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL---EEKKEKLQEEEDKLL------EEAEKEAQQA 578
|
90 100
....*....|....*....|....*.
gi 1958778166 428 REELKKNytgQNVISKTLREKNKLEN 453
Cdd:PRK00409 579 IKEAKKE---ADEIIKELRQLQKGGY 601
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
5-95 |
3.59e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 38.96 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 5 LKSPDGFFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNEAEGTFV--LQDFNTRNGTFVNECHI-QNVAVKLIPGDI 81
Cdd:cd22681 36 LNSPSCYLIGREKGESTEIVVADIGIPEETCSKQHCVIQFRNVKGILKpyIMDLDSSNGTCLNDNVIpSSRYVELRSGDV 115
|
90
....*....|....
gi 1958778166 82 LRFgSSGPTYELVI 95
Cdd:cd22681 116 ITF-SKSNDYELVF 128
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
624-836 |
3.68e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 624 LETQQSLQEENLAEKE-KLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLqGDLEMTQARvheLENDLA-CQKEV- 700
Cdd:PHA02562 204 IEEQRKKNGENIARKQnKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAK---IKSKIEqFQKVIk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 701 -LES-----SVTQEKRKMREVLEAERRKAQDLENQLTQQKEisesnTYEKLKMR-DTLEKEKRRIQDLENRLTKQREEIE 773
Cdd:PHA02562 280 mYEKggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDT-----AIDELEEImDEFNEQSKKLLELKNKISTNKQSLI 354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778166 774 LkgqkediLNNKLKDALLLVEDAQQMRTAESTRAEKLS---LKLKETLAELEITKAKMIMAEDRLK 836
Cdd:PHA02562 355 T-------LVDKAKKVKAAIEELQAEFVDNAEELAKLQdelDKIVKTKSELVKEKYHRGIVTDLLK 413
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
246-434 |
3.78e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 246 IMNLQAEIADLSQRLSEmaavvaAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQvLSQTLAERNTEIES 325
Cdd:TIGR04523 386 IKNLESQINDLESKIQN------QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKN 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 326 LKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREa 405
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE- 537
|
170 180
....*....|....*....|....*....
gi 1958778166 406 qekelklcrSQMQDMEKEVKKLREELKKN 434
Cdd:TIGR04523 538 ---------SKISDLEDELNKDDFELKKE 557
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
603-771 |
3.82e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 603 LEHYKKIMIQSEElraqvnasletQQSLQEENLAEKEKLteKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEm 682
Cdd:pfam17380 398 LEAARKVKILEEE-----------RQRKIQQQKVEMEQI--RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVE- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 683 tqaRVHELENDLACQKEVLEssvtQEKRKMREVlEAERRKAQDLENQLTQQKEISESNTYEKL------KMRDTLEKEKR 756
Cdd:pfam17380 464 ---RLRQQEEERKRKKLELE----KEKRDRKRA-EEQRRKILEKELEERKQAMIEEERKRKLLekemeeRQKAIYEEERR 535
|
170
....*....|....*
gi 1958778166 757 RIQDLENRLTKQREE 771
Cdd:pfam17380 536 REAEEERRKQQEMEE 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
628-771 |
3.99e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 628 QSLQEEnLAEKEKLTEKLEQE----EKLKARIQQLTEEKAALEEsvaeEKNKLQGDLEMTQARVHELENDLACQKEVLES 703
Cdd:COG4913 664 ASAERE-IAELEAELERLDASsddlAALEEQLEELEAELEELEE----ELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778166 704 SVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESntyeklkmrdtLEKEKRRIQDLENRLTKQREE 771
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEER-----------IDALRARLNRAEEELERAMRA 795
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
574-866 |
4.12e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.21 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 574 LEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKImiqsEELRAQVNASLETQQSLQEEN------LAEKEKLTEKLEQ 647
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELRDKTAQA----EALERQLAAETEQNRALEEENkalreeAQAAEKALQRAEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 648 E-----------EKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQ--------- 707
Cdd:pfam19220 161 ElatarerlallEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQleeaveahr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 708 -EKRKMREVLEAERRKAQDLENQLTQQKE----------ISESNTYEKLKMRDTLEkekRRIQDLENRLTKQREEielkg 776
Cdd:pfam19220 241 aERASLRMKLEALTARAAATEQLLAEARNqlrdrdeairAAERRLKEASIERDTLE---RRLAGLEADLERRTQQ----- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 777 qkedilnnklkdalllVEDAQQMRTAESTRAEKLSLKLKETLAELEitkakmiMAEDRLKLQQQSMKALQDERESQKHGF 856
Cdd:pfam19220 313 ----------------FQEMQRARAELEERAEMLTKALAAKDAALE-------RAEERIASLSDRIAELTKRFEVERAAL 369
|
330
....*....|
gi 1958778166 857 EEEITEYKEQ 866
Cdd:pfam19220 370 EQANRRLKEE 379
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
564-1131 |
4.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 564 LNILRVSLSWLEETEQLLGDLNIELSDSDKGFSLcliyLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTE 643
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ----LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 644 KLEQEEKLKARIQQLTEEKAALEESVAEEKN--------KLQGDLEMTQARVHELENDLAcQKEVLESSVTQEKRKMREV 715
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkELKSELKNQEKKLEEIQNQIS-QNNKIISQLNEQISQLKKE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 716 LEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDilnnKLKDALLLVED 795
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK----KLQQEKELLEK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 796 AQQMRTAESTRAEKLSLKLKETLAELEITKAKMimaEDRLKLQQQSMKALQDERESQKHGFEE----------EITEYKE 865
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNL---DNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekELKKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 866 QIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVpqeFTIVPSLDSSAKEIACDHL---IDDLLMAQKEI 942
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL---NKDDFELKKENLEKEIDEKnkeIEELKQTQKSL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 943 LSQQEiimKLRTDLGEAHTRMSDLRGELSEKQKT--ELERQVALVRQQNSELSILKAKVVQTTglvEKKDRELKVLREAL 1020
Cdd:TIGR04523 581 KKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKisSLEKELEKAKKENEKLSSIIKNIKSKK---NKLKQEVKQIKETI 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 1021 RASQEKprpYLSTEQKPRNLSQKCDislqiepahpdsfssfqeeqffsdlgakckgsrheEVIQRQKKALSELRTRIKEl 1100
Cdd:TIGR04523 655 KEIRNK---WPEIIKKIKESKTKID-----------------------------------DIIELMKDWLKELSLHYKK- 695
|
570 580 590
....*....|....*....|....*....|.
gi 1958778166 1101 ekaNSSNHKDHVNESFLELKTLRMEKNVQKI 1131
Cdd:TIGR04523 696 ---YITRMIRIKDLPKLEEKYKEIEKELKKL 723
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
710-900 |
4.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 710 RKMREVLEAERRKAQDL----ENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNK 785
Cdd:COG4913 238 ERAHEALEDAREQIELLepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 786 LKDALLLVEDAQQMRTAESTRAEKlslKLKETLAELEITKAKmimAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKE 865
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEE---RERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*
gi 1958778166 866 QIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKD 900
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
246-665 |
4.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 246 IMNLQaEIADLSQRLSEMAAVVAAARQSNRcdpRFQDLDEGDDHRQKEIESMKSQINALQKGYSQV-LSQTLAERNTEIE 324
Cdd:COG4717 67 ELNLK-ELKELEEELKEAEEKEEEYAELQE---ELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 325 SLKNEGENLKRDQAitsgMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEyqLEALTSRCSKLkEDLRKEEAQ-KERR 403
Cdd:COG4717 143 ELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLAT--EEELQDLAEEL-EELQQRLAElEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 404 EAQEKELKLCRSQMQDMEKE--VKKLREELKKNYTGQNVISKTLR---EKNKLENFRSQVIKATF--------GKTKPFR 470
Cdd:COG4717 216 EEAQEELEELEEELEQLENEleAAALEERLKEARLLLLIAAALLAllgLGGSLLSLILTIAGVLFlvlgllalLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 471 DKPVTDQQLIERIVQVTEDNLsfQQRKWTLQRETHLHSKQEEVVHNVEKLRVLLDKCQACMRDScnsmDLKKEVELLQHL 550
Cdd:COG4717 296 EKASLGKEAEELQALPALEEL--EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE----ELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 551 QLSPPVLGLQKAV-LNILRVSLSWLEETEQL---LGDLNIELSDSDKGFSLCLIY-----LLEHYKKIMIQSEELRAQVN 621
Cdd:COG4717 370 QEIAALLAEAGVEdEEELRAALEQAEEYQELkeeLEELEEQLEELLGELEELLEAldeeeLEEELEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958778166 622 ASLETQQSLQEE--NLAEKEKLTEKLEQEEKLKARIQQLTEEKAAL 665
Cdd:COG4717 450 ELREELAELEAEleQLEEDGELAELLQELEELKAELRELAEEWAAL 495
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
618-1126 |
4.74e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 618 AQVNASLETQQSLQEENLAEKEKLTEKLEQE--EKLKARIQQLTEEKAALEESVAEEKNKLQGDlemtqarvhELENDLA 695
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDDLQALESElrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQA---------TATPELL 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 696 CQKEVLESSVtqekRKMREVLEAERRKAQDLENQLTQQKEISEsntyeklKMRDTLEKEKRRIQDLENRLTKQREEIELK 775
Cdd:pfam12128 464 LQLENFDERI----ERAREEQEAANAEVERLQSELRQARKRRD-------QASEALRQASRRLEERQSALDELELQLFPQ 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 776 -GQKEDILNNKLKD-----------ALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSmK 843
Cdd:pfam12128 533 aGTLLHFLRKEAPDweqsigkvispELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAE-E 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 844 ALQDERESQKHGFEE------EITEYKEQIKQHSQTIVNLEERLSQVTqyyrkieGEIATLKDS-DSAQKEEVPQEFTIV 916
Cdd:pfam12128 612 ALQSAREKQAAAEEQlvqangELEKASREETFARTALKNARLDLRRLF-------DEKQSEKDKkNKALAERKDSANERL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 917 PSLDSSAKEiacdhliddLLMAQKEILSQQeiimklRTDLGEAHTRMSDLRGELSEKQKTELERqvaLVRQQNSELSILK 996
Cdd:pfam12128 685 NSLEAQLKQ---------LDKKHQAWLEEQ------KEQKREARTEKQAYWQVVEGALDAQLAL---LKAAIAARRSGAK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 997 AkvvQTTGLVEKKDRELKVLrealrasQEKPRPYLSTEQKPRNLSQKCDislQIEPAHPD--SFSSFQEEQFFSD---LG 1071
Cdd:pfam12128 747 A---ELKALETWYKRDLASL-------GVDPDVIAKLKREIRTLERKIE---RIAVRRQEvlRYFDWYQETWLQRrprLA 813
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778166 1072 AKCKGSRHE--EVIQRQKKALSELRTRIKELEKANSSNHK--DHVNESFLELKtLRMEK 1126
Cdd:pfam12128 814 TQLSNIERAisELQQQLARLIADTKLRRAKLEMERKASEKqqVRLSENLRGLR-CEMSK 871
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-874 |
5.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 707 QEKRKMREVLEAERRKAQDLENQLTQQKEisesntyeklKMRDTLEKEKRRIQDLENRLTKQREEIE-LKGQKEDILNNK 785
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 786 LKDALLLVEDAQQMRTAEstrAEKLSLKLKETLAELEITKAKmimAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKE 865
Cdd:COG1579 90 EYEALQKEIESLKRRISD---LEDEILELMERIEELEEELAE---LEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*....
gi 1958778166 866 QIKQHSQTI 874
Cdd:COG1579 164 EREELAAKI 172
|
|
| FHA_RAD53-like_rpt1 |
cd22689 |
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
13-93 |
5.55e-03 |
|
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438741 [Multi-domain] Cd Length: 132 Bit Score: 38.41 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 13 VLKKSTTIGKHEDSDLVLQSSDIDNHHALI---EFNEAEGTFVLQDFNTrNGTFVNEchiQNVAVK----LIPGDILRFG 85
Cdd:cd22689 42 SIKKVWTFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDISS-NGTWLNG---QRLEKNsnqlLSQGDEITIG 117
|
....*...
gi 1958778166 86 SSGPTYEL 93
Cdd:cd22689 118 VGVTGDIL 125
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
264-446 |
5.77e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 264 AAVVAAARQSNR--CDpRFQ-----DL-DEGDDHRQKEIESMKSQINALQKgysqvlsqtlaerntEIESLKNEGENLKR 335
Cdd:COG0542 369 EALVAAVRLSDRyiTD-RFLpdkaiDLiDEAAARVRMEIDSKPEELDELER---------------RLEQLEIEKEALKK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 336 DQAITSgmvtslQKDVSARNEQVQQLQEEVNQLRIQ-NKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKLCR 414
Cdd:COG0542 433 EQDEAS------FERLAELRDELAELEEELEALKARwEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 415 -----------------------SQMQDMEKE-VKKLREELKKNYTGQN----VISKTLR 446
Cdd:COG0542 507 llreevteediaevvsrwtgipvGKLLEGEREkLLNLEEELHERVIGQDeaveAVADAIR 566
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
614-669 |
5.97e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 36.86 E-value: 5.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778166 614 EELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESV 669
Cdd:pfam06005 7 EQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERI 62
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
603-906 |
6.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 603 LEHYKKIMIQSEELRAQVNASLETQQSLQEE--NLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNkLQGDL 680
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE-LEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 681 EMTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISES--NTYEKLKMRDTLEKEKRRI 758
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEleEELEQLENELEAAALEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 759 QDLENRL------------------------------------------------TKQREEIELKGQKEDILNNKLK--- 787
Cdd:COG4717 246 KEARLLLliaaallallglggsllsliltiagvlflvlgllallflllarekaslGKEAEELQALPALEELEEEELEell 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 788 ---------------DALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKL--QQQSMKALQDERE 850
Cdd:COG4717 326 aalglppdlspeellELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAleQAEEYQELKEELE 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778166 851 SQKHGFEEEITEY------------KEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQK 906
Cdd:COG4717 406 ELEEQLEELLGELeellealdeeelEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-433 |
6.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 346 SLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQkerREAQEKELKLCRSQMQDMEKEVK 425
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAELRAELE 100
|
....*...
gi 1958778166 426 KLREELKK 433
Cdd:COG4942 101 AQKEELAE 108
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
351-446 |
6.39e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 351 VSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQ----EKELKLCRSQMQDMEKEVKK 426
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAE 94
|
90 100
....*....|....*....|
gi 1958778166 427 LREELKKNytgQNVISKTLR 446
Cdd:COG4942 95 LRAELEAQ---KEELAELLR 111
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
612-745 |
6.52e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 612 QSEELRAQVNASLETQQSLQEEnlaekekLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELE 691
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEE-------ITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELE 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958778166 692 NDLacqkevlessvtqekRKMREVLEAERRKAQDLEN-QLTQQKEIsesNTYEKL 745
Cdd:pfam00038 270 AEL---------------QETRQEMARQLREYQELLNvKLALDIEI---ATYRKL 306
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
614-719 |
7.57e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 614 EELRAQVNAsLETqqslqEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELEND 693
Cdd:COG0542 414 DELERRLEQ-LEI-----EKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100
....*....|....*....|....*...
gi 1958778166 694 LACQKEV--LESSVTQEKRKMREVLEAE 719
Cdd:COG0542 488 PELEKELaeLEEELAELAPLLREEVTEE 515
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
264-419 |
7.97e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 264 AAVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQV---LSQTLAERnteIESLKNEGENLKRDQAIT 340
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnllADETLADR---LEELREELDAAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 341 S----------GMVTSLQKDvsarNEQVQQLQEEVNQLRIQNKEKEYQLEALT------------------SRCSKLKED 392
Cdd:COG3096 913 QqhgkalaqlePLVAVLQSD----PEQFEQLQADYLQAKEQQRRLKQQIFALSevvqrrphfsyedavgllGENSDLNEK 988
|
170 180
....*....|....*....|....*....
gi 1958778166 393 LRK--EEAQKERREAQEKeLKLCRSQMQD 419
Cdd:COG3096 989 LRArlEQAEEARREAREQ-LRQAQAQYSQ 1016
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
613-841 |
8.16e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 613 SEELRAQVNA---SLETQQSLQEENLAEKEKLTEKLE-QEEKLKARIQQLTEEKAALEESVAEEKnklqgdLEMTQARVH 688
Cdd:PRK11281 190 RPSQRVLLQAeqaLLNAQNDLQRKSLEGNTQLQDLLQkQRDYLTARIQRLEHQLQLLQEAINSKR------LTLSEKTVQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 689 ELENDLACQKEVLESSVTQEkrkmrevLEAERR------KAQDLENQLTQQ----KEI------SESNTYEKLK-MRDTL 751
Cdd:PRK11281 264 EAQSQDEAARIQANPLVAQE-------LEINLQlsqrllKATEKLNTLTQQnlrvKNWldrltqSERNIKEQISvLKGSL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 752 --------EKEK----RRIQDLENR----------LTKQREEIE---------LKGQKEDIlNNKLKDALLLVEDaqqmr 800
Cdd:PRK11281 337 llsrilyqQQQAlpsaDLIEGLADRiadlrleqfeINQQRDALFqpdayidklEAGHKSEV-TDEVRDALLQLLD----- 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958778166 801 taesTRAEKLSLKLKE-----TLA-ELEITKAKMIMAEDRL--KLQQQS 841
Cdd:PRK11281 411 ----ERRELLDQLNKQlnnqlNLAiNLQLNQQQLLSVSDSLqsTLTQQI 455
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
832-1025 |
8.57e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 832 EDRLKLQQQSMKALQDERES--QKHGfeeeITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEV 909
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEfrQKNG----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 910 PqeftivpsldssakEIACDHLIDDLLMAQKEILSQqeiIMKLRTDLGEAHTRMSDLRGELSE----------KQKTELE 979
Cdd:COG3206 257 P--------------ELLQSPVIQQLRAQLAELEAE---LAELSARYTPNHPDVIALRAQIAAlraqlqqeaqRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958778166 980 RQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQE 1025
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
290-408 |
8.71e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 290 RQKEIESMKSQIN------ALQKGYSQVLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDV----SARNEQVQ 359
Cdd:PRK09039 51 KDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAgelaQELDSEKQ 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958778166 360 QLQEEVNQLRIQNKekeyQLEALTSRCSKLKEDLrkEEAQKERREAQEK 408
Cdd:PRK09039 131 VSARALAQVELLNQ----QIAALRRQLAALEAAL--DASEKRDRESQAK 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-432 |
9.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 298 KSQINALQKGYSQvLSQTLAERNTEIESLKNEGENL--KRDQAITSGMVTSLQKDVSARNEQVQQLQEevnqlriqnkek 375
Cdd:COG4913 609 RAKLAALEAELAE-LEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEA------------ 675
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778166 376 eyQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELK 432
Cdd:COG4913 676 --ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
617-946 |
9.58e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 617 RAQVNASLETQQSlQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAeeknklQGDLEMTQARvheleNDLAC 696
Cdd:PRK11281 38 EADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLA------QAPAKLRQAQ-----AELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 697 QKEVLESSVTQEKRKMrEVLEAERRKAQDLENQLTQQKEISESNTyeKL--------KMRDTLEKEKRRIQDLENRLTKQ 768
Cdd:PRK11281 106 LKDDNDEETRETLSTL-SLRQLESRLAQTLDQLQNAQNDLAEYNS--QLvslqtqpeRAQAALYANSQRLQQIRNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 769 R-EEIELKGQKEDILNNKLkdALL---------LVEDAQQMRTAESTRAEKLSLKLkeTLAELEITKAKMIMAEDRLKLQ 838
Cdd:PRK11281 183 KvGGKALRPSQRVLLQAEQ--ALLnaqndlqrkSLEGNTQLQDLLQKQRDYLTARI--QRLEHQLQLLQEAINSKRLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778166 839 QQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEER---LSQ-----------VTQYYRKIEGEIATLKDS--- 901
Cdd:PRK11281 259 EKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKlntLTQqnlrvknwldrLTQSERNIKEQISVLKGSlll 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958778166 902 ---DSAQKEEVPQeftivPSLDSS-AKEIAcdhlidDLLMAQKEIlSQQ 946
Cdd:PRK11281 339 sriLYQQQQALPS-----ADLIEGlADRIA------DLRLEQFEI-NQQ 375
|
|
| |
